Copper in PDB 1kya: Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
Enzymatic activity of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
All present enzymatic activity of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine:
1.10.3.2;
Protein crystallography data
The structure of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine, PDB code: 1kya
was solved by
T.Bertrand,
C.Jolivalt,
P.Briozzo,
E.Caminade,
N.Joly,
C.Madzak,
C.Mougin,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
35.00 /
2.40
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
87.720,
110.520,
123.201,
90.00,
103.44,
90.00
|
|
R / Rfree (%)
|
25.3 /
27.6
|
Copper Binding Sites:
The binding sites of Copper atom in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
(pdb code 1kya). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 16 binding sites of Copper where determined in the
Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine, PDB code: 1kya:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
11;
12;
13;
14;
15;
16;
Copper binding site 1 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 1 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu500
b:47.3
occ:1.00
|
SG
|
A:CYS453
|
2.2
|
41.0
|
1.0
|
|
ND1
|
A:HIS458
|
2.2
|
45.9
|
1.0
|
|
ND1
|
A:HIS395
|
2.4
|
38.6
|
1.0
|
|
CE1
|
A:HIS458
|
3.1
|
46.3
|
1.0
|
|
CG
|
A:HIS458
|
3.2
|
44.0
|
1.0
|
|
CG
|
A:HIS395
|
3.2
|
37.2
|
1.0
|
|
CB
|
A:CYS453
|
3.3
|
36.7
|
1.0
|
|
CE1
|
A:HIS395
|
3.3
|
38.4
|
1.0
|
|
CB
|
A:HIS395
|
3.4
|
36.1
|
1.0
|
|
CD1
|
A:ILE455
|
3.5
|
35.0
|
1.0
|
|
CB
|
A:HIS458
|
3.6
|
41.3
|
1.0
|
|
CD2
|
A:PHE463
|
3.7
|
38.2
|
1.0
|
|
CB
|
A:ILE455
|
3.8
|
36.0
|
1.0
|
|
CE2
|
A:PHE463
|
3.8
|
37.7
|
1.0
|
|
CG1
|
A:ILE455
|
3.9
|
37.4
|
1.0
|
|
CA
|
A:HIS395
|
3.9
|
35.5
|
1.0
|
|
NE2
|
A:HIS458
|
4.3
|
46.9
|
1.0
|
|
CD2
|
A:HIS458
|
4.3
|
45.8
|
1.0
|
|
CD2
|
A:HIS395
|
4.4
|
37.9
|
1.0
|
|
NE2
|
A:HIS395
|
4.4
|
40.2
|
1.0
|
|
CD
|
A:PRO396
|
4.5
|
34.0
|
1.0
|
|
CG2
|
A:ILE455
|
4.6
|
34.8
|
1.0
|
|
CA
|
A:CYS453
|
4.7
|
36.2
|
1.0
|
|
N
|
A:ILE455
|
4.8
|
35.9
|
1.0
|
|
C
|
A:HIS395
|
4.8
|
35.2
|
1.0
|
|
CA
|
A:ILE455
|
4.9
|
36.2
|
1.0
|
|
O
|
A:GLY392
|
4.9
|
42.1
|
1.0
|
|
N
|
A:HIS395
|
5.0
|
35.6
|
1.0
|
|
N
|
A:PRO396
|
5.0
|
34.8
|
1.0
|
|
O
|
A:ILE455
|
5.0
|
35.5
|
1.0
|
|
CG
|
A:PHE463
|
5.0
|
37.1
|
1.0
|
|
Copper binding site 2 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 2 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:43.8
occ:1.00
|
O
|
A:HOH1505
|
1.8
|
38.1
|
1.0
|
|
NE2
|
A:HIS400
|
2.1
|
30.7
|
1.0
|
|
NE2
|
A:HIS452
|
2.2
|
36.0
|
1.0
|
|
NE2
|
A:HIS111
|
2.3
|
31.4
|
1.0
|
|
CE1
|
A:HIS400
|
2.9
|
28.9
|
1.0
|
|
CE1
|
A:HIS452
|
3.0
|
35.6
|
1.0
|
|
CD2
|
A:HIS111
|
3.2
|
31.6
|
1.0
|
|
CD2
|
A:HIS400
|
3.2
|
30.7
|
1.0
|
|
CE1
|
A:HIS111
|
3.3
|
31.3
|
1.0
|
|
CD2
|
A:HIS452
|
3.4
|
36.2
|
1.0
|
|
CD2
|
A:HIS398
|
3.6
|
37.7
|
1.0
|
|
CU
|
A:CU502
|
3.8
|
48.3
|
1.0
|
|
CU
|
A:CU503
|
4.0
|
76.1
|
1.0
|
|
ND1
|
A:HIS400
|
4.1
|
31.2
|
1.0
|
|
ND1
|
A:HIS452
|
4.2
|
35.6
|
1.0
|
|
NE2
|
A:HIS398
|
4.2
|
39.6
|
1.0
|
|
CG
|
A:HIS400
|
4.3
|
32.0
|
1.0
|
|
CG
|
A:HIS111
|
4.4
|
31.1
|
1.0
|
|
ND1
|
A:HIS111
|
4.4
|
31.4
|
1.0
|
|
CG
|
A:HIS452
|
4.4
|
35.4
|
1.0
|
|
CD2
|
A:HIS64
|
4.4
|
37.5
|
1.0
|
|
NE2
|
A:HIS64
|
4.7
|
39.3
|
1.0
|
|
CG
|
A:HIS398
|
4.7
|
38.2
|
1.0
|
|
NE2
|
A:HIS454
|
4.8
|
32.8
|
1.0
|
|
CD2
|
A:HIS454
|
4.8
|
32.3
|
1.0
|
|
CD2
|
A:PHE450
|
4.8
|
33.5
|
1.0
|
|
CG
|
A:HIS64
|
4.9
|
37.1
|
1.0
|
|
CB
|
A:PHE450
|
5.0
|
34.9
|
1.0
|
|
Copper binding site 3 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 3 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:48.3
occ:1.00
|
O
|
A:HOH1505
|
2.1
|
38.1
|
1.0
|
|
NE2
|
A:HIS454
|
2.3
|
32.8
|
1.0
|
|
ND1
|
A:HIS66
|
2.3
|
35.2
|
1.0
|
|
NE2
|
A:HIS109
|
2.5
|
30.1
|
1.0
|
|
CE1
|
A:HIS66
|
2.9
|
34.6
|
1.0
|
|
CD2
|
A:HIS454
|
3.1
|
32.3
|
1.0
|
|
CE1
|
A:HIS109
|
3.3
|
29.6
|
1.0
|
|
CE1
|
A:HIS454
|
3.4
|
31.8
|
1.0
|
|
CG
|
A:HIS66
|
3.4
|
33.6
|
1.0
|
|
CD2
|
A:HIS109
|
3.7
|
28.9
|
1.0
|
|
CD2
|
A:HIS64
|
3.7
|
37.5
|
1.0
|
|
CU
|
A:CU503
|
3.8
|
76.1
|
1.0
|
|
CU
|
A:CU501
|
3.8
|
43.8
|
1.0
|
|
CD2
|
A:HIS398
|
4.0
|
37.7
|
1.0
|
|
CB
|
A:HIS66
|
4.0
|
32.8
|
1.0
|
|
NE2
|
A:HIS66
|
4.1
|
34.2
|
1.0
|
|
NE2
|
A:HIS398
|
4.1
|
39.6
|
1.0
|
|
CZ2
|
A:TRP107
|
4.2
|
30.6
|
1.0
|
|
NE2
|
A:HIS64
|
4.3
|
39.3
|
1.0
|
|
CG
|
A:HIS454
|
4.3
|
33.0
|
1.0
|
|
CD2
|
A:HIS66
|
4.4
|
33.9
|
1.0
|
|
ND1
|
A:HIS454
|
4.4
|
32.1
|
1.0
|
|
ND1
|
A:HIS109
|
4.5
|
31.0
|
1.0
|
|
CB
|
A:ALA241
|
4.6
|
28.9
|
1.0
|
|
CE2
|
A:TRP107
|
4.6
|
29.7
|
1.0
|
|
CG
|
A:HIS109
|
4.7
|
30.0
|
1.0
|
|
CH2
|
A:TRP107
|
4.8
|
28.9
|
1.0
|
|
CG
|
A:HIS64
|
4.8
|
37.1
|
1.0
|
|
NE1
|
A:TRP107
|
4.8
|
28.0
|
1.0
|
|
CA
|
A:HIS66
|
4.9
|
32.2
|
1.0
|
|
CD2
|
A:HIS111
|
4.9
|
31.6
|
1.0
|
|
CG
|
A:HIS398
|
4.9
|
38.2
|
1.0
|
|
NE2
|
A:HIS111
|
4.9
|
31.4
|
1.0
|
|
Copper binding site 4 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 4 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:76.1
occ:1.00
|
NE2
|
A:HIS398
|
2.0
|
39.6
|
1.0
|
|
NE2
|
A:HIS64
|
2.1
|
39.3
|
1.0
|
|
O
|
A:HOH1540
|
2.6
|
36.9
|
1.0
|
|
CD2
|
A:HIS398
|
2.9
|
37.7
|
1.0
|
|
CE1
|
A:HIS64
|
3.0
|
37.1
|
1.0
|
|
CE1
|
A:HIS398
|
3.0
|
38.7
|
1.0
|
|
CD2
|
A:HIS64
|
3.0
|
37.5
|
1.0
|
|
CE1
|
A:HIS400
|
3.3
|
28.9
|
1.0
|
|
O
|
A:HOH1505
|
3.4
|
38.1
|
1.0
|
|
NE2
|
A:HIS400
|
3.5
|
30.7
|
1.0
|
|
ND1
|
A:HIS400
|
3.5
|
31.2
|
1.0
|
|
ND1
|
A:HIS66
|
3.7
|
35.2
|
1.0
|
|
CG
|
A:HIS66
|
3.8
|
33.6
|
1.0
|
|
CU
|
A:CU502
|
3.8
|
48.3
|
1.0
|
|
CD2
|
A:HIS400
|
3.8
|
30.7
|
1.0
|
|
CG
|
A:HIS400
|
3.8
|
32.0
|
1.0
|
|
CE1
|
A:HIS66
|
3.9
|
34.6
|
1.0
|
|
CA
|
A:HIS66
|
4.0
|
32.2
|
1.0
|
|
CU
|
A:CU501
|
4.0
|
43.8
|
1.0
|
|
CD2
|
A:HIS66
|
4.0
|
33.9
|
1.0
|
|
ND1
|
A:HIS64
|
4.0
|
37.9
|
1.0
|
|
CG
|
A:HIS64
|
4.1
|
37.1
|
1.0
|
|
ND1
|
A:HIS398
|
4.1
|
38.7
|
1.0
|
|
CG
|
A:HIS398
|
4.1
|
38.2
|
1.0
|
|
NE2
|
A:HIS66
|
4.1
|
34.2
|
1.0
|
|
N
|
A:GLY67
|
4.2
|
32.9
|
1.0
|
|
CB
|
A:HIS66
|
4.3
|
32.8
|
1.0
|
|
C
|
A:HIS66
|
4.6
|
32.6
|
1.0
|
|
CA
|
A:HIS400
|
4.7
|
34.0
|
1.0
|
|
CB
|
A:HIS400
|
4.8
|
32.9
|
1.0
|
|
N
|
A:HIS66
|
4.8
|
32.2
|
1.0
|
|
O
|
A:LEU399
|
4.9
|
35.5
|
1.0
|
|
Copper binding site 5 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 5 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu500
b:48.8
occ:1.00
|
ND1
|
B:HIS458
|
2.2
|
45.0
|
1.0
|
|
SG
|
B:CYS453
|
2.2
|
41.0
|
1.0
|
|
ND1
|
B:HIS395
|
2.4
|
38.4
|
1.0
|
|
CE1
|
B:HIS458
|
3.1
|
45.2
|
1.0
|
|
CG
|
B:HIS458
|
3.2
|
43.6
|
1.0
|
|
CG
|
B:HIS395
|
3.3
|
38.1
|
1.0
|
|
CE1
|
B:HIS395
|
3.3
|
37.6
|
1.0
|
|
CB
|
B:CYS453
|
3.3
|
36.2
|
1.0
|
|
CB
|
B:HIS458
|
3.5
|
41.6
|
1.0
|
|
CB
|
B:HIS395
|
3.5
|
36.5
|
1.0
|
|
CD1
|
B:ILE455
|
3.6
|
34.3
|
1.0
|
|
CD2
|
B:PHE463
|
3.7
|
37.6
|
1.0
|
|
CB
|
B:ILE455
|
3.8
|
36.1
|
1.0
|
|
CE2
|
B:PHE463
|
3.8
|
37.4
|
1.0
|
|
CG1
|
B:ILE455
|
3.9
|
35.8
|
1.0
|
|
CA
|
B:HIS395
|
4.0
|
35.9
|
1.0
|
|
NE2
|
B:HIS458
|
4.2
|
45.4
|
1.0
|
|
CD2
|
B:HIS458
|
4.3
|
44.7
|
1.0
|
|
NE2
|
B:HIS395
|
4.4
|
39.9
|
1.0
|
|
CD2
|
B:HIS395
|
4.4
|
37.7
|
1.0
|
|
CG2
|
B:ILE455
|
4.5
|
36.4
|
1.0
|
|
CD
|
B:PRO396
|
4.6
|
34.9
|
1.0
|
|
CA
|
B:CYS453
|
4.7
|
36.1
|
1.0
|
|
N
|
B:ILE455
|
4.8
|
36.1
|
1.0
|
|
CA
|
B:ILE455
|
4.8
|
36.7
|
1.0
|
|
O
|
B:ILE455
|
4.9
|
36.2
|
1.0
|
|
C
|
B:HIS395
|
4.9
|
36.0
|
1.0
|
|
CG
|
B:PHE463
|
5.0
|
38.0
|
1.0
|
|
CA
|
B:HIS458
|
5.0
|
39.9
|
1.0
|
|
Copper binding site 6 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 6 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu501
b:46.2
occ:1.00
|
O
|
B:HOH1502
|
1.9
|
45.9
|
1.0
|
|
NE2
|
B:HIS400
|
2.2
|
31.2
|
1.0
|
|
NE2
|
B:HIS452
|
2.2
|
34.8
|
1.0
|
|
NE2
|
B:HIS111
|
2.3
|
30.4
|
1.0
|
|
CE1
|
B:HIS452
|
2.9
|
35.5
|
1.0
|
|
CE1
|
B:HIS400
|
3.0
|
29.0
|
1.0
|
|
CD2
|
B:HIS111
|
3.2
|
30.3
|
1.0
|
|
CD2
|
B:HIS400
|
3.3
|
30.1
|
1.0
|
|
CE1
|
B:HIS111
|
3.4
|
30.9
|
1.0
|
|
CD2
|
B:HIS452
|
3.4
|
35.5
|
1.0
|
|
CD2
|
B:HIS398
|
3.5
|
38.4
|
1.0
|
|
CU
|
B:CU503
|
3.9
|
74.7
|
1.0
|
|
CU
|
B:CU502
|
4.0
|
50.4
|
1.0
|
|
ND1
|
B:HIS452
|
4.1
|
36.6
|
1.0
|
|
ND1
|
B:HIS400
|
4.2
|
30.3
|
1.0
|
|
NE2
|
B:HIS398
|
4.2
|
41.3
|
1.0
|
|
CG
|
B:HIS400
|
4.3
|
31.7
|
1.0
|
|
CG
|
B:HIS111
|
4.4
|
30.9
|
1.0
|
|
CD2
|
B:HIS64
|
4.4
|
37.9
|
1.0
|
|
ND1
|
B:HIS111
|
4.4
|
31.7
|
1.0
|
|
CG
|
B:HIS452
|
4.4
|
35.5
|
1.0
|
|
NE2
|
B:HIS64
|
4.6
|
39.7
|
1.0
|
|
CG
|
B:HIS398
|
4.7
|
38.2
|
1.0
|
|
NE2
|
B:HIS454
|
4.7
|
30.7
|
1.0
|
|
CD2
|
B:HIS454
|
4.7
|
31.3
|
1.0
|
|
CD2
|
B:PHE450
|
4.9
|
33.8
|
1.0
|
|
CG
|
B:HIS64
|
4.9
|
36.9
|
1.0
|
|
CE1
|
B:HIS109
|
5.0
|
29.3
|
1.0
|
|
Copper binding site 7 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 7 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu502
b:50.4
occ:1.00
|
O
|
B:HOH1502
|
2.1
|
45.9
|
1.0
|
|
ND1
|
B:HIS66
|
2.2
|
33.9
|
1.0
|
|
NE2
|
B:HIS454
|
2.2
|
30.7
|
1.0
|
|
NE2
|
B:HIS109
|
2.4
|
30.3
|
1.0
|
|
CE1
|
B:HIS66
|
2.9
|
34.9
|
1.0
|
|
CD2
|
B:HIS454
|
3.1
|
31.3
|
1.0
|
|
CE1
|
B:HIS454
|
3.2
|
31.0
|
1.0
|
|
CE1
|
B:HIS109
|
3.3
|
29.3
|
1.0
|
|
CG
|
B:HIS66
|
3.3
|
32.8
|
1.0
|
|
CD2
|
B:HIS109
|
3.5
|
30.1
|
1.0
|
|
CD2
|
B:HIS64
|
3.8
|
37.9
|
1.0
|
|
CU
|
B:CU503
|
3.9
|
74.7
|
1.0
|
|
CB
|
B:HIS66
|
3.9
|
33.2
|
1.0
|
|
CZ2
|
B:TRP107
|
3.9
|
30.5
|
1.0
|
|
CU
|
B:CU501
|
4.0
|
46.2
|
1.0
|
|
NE2
|
B:HIS66
|
4.1
|
34.9
|
1.0
|
|
CD2
|
B:HIS398
|
4.2
|
38.4
|
1.0
|
|
CG
|
B:HIS454
|
4.3
|
32.8
|
1.0
|
|
CD2
|
B:HIS66
|
4.3
|
34.5
|
1.0
|
|
NE2
|
B:HIS398
|
4.3
|
41.3
|
1.0
|
|
ND1
|
B:HIS454
|
4.3
|
31.9
|
1.0
|
|
CE2
|
B:TRP107
|
4.4
|
28.9
|
1.0
|
|
NE2
|
B:HIS64
|
4.4
|
39.7
|
1.0
|
|
CB
|
B:ALA241
|
4.4
|
28.9
|
1.0
|
|
ND1
|
B:HIS109
|
4.5
|
29.9
|
1.0
|
|
CH2
|
B:TRP107
|
4.5
|
29.0
|
1.0
|
|
NE1
|
B:TRP107
|
4.6
|
27.2
|
1.0
|
|
CG
|
B:HIS109
|
4.6
|
29.5
|
1.0
|
|
CA
|
B:HIS66
|
4.8
|
33.0
|
1.0
|
|
CG
|
B:HIS64
|
5.0
|
36.9
|
1.0
|
|
Copper binding site 8 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 8 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu503
b:74.7
occ:1.00
|
NE2
|
B:HIS398
|
2.0
|
41.3
|
1.0
|
|
NE2
|
B:HIS64
|
2.0
|
39.7
|
1.0
|
|
O
|
B:HOH1304
|
2.3
|
68.8
|
1.0
|
|
CD2
|
B:HIS64
|
2.9
|
37.9
|
1.0
|
|
CD2
|
B:HIS398
|
2.9
|
38.4
|
1.0
|
|
CE1
|
B:HIS64
|
3.0
|
38.0
|
1.0
|
|
CE1
|
B:HIS398
|
3.1
|
39.7
|
1.0
|
|
CE1
|
B:HIS400
|
3.2
|
29.0
|
1.0
|
|
ND1
|
B:HIS400
|
3.5
|
30.3
|
1.0
|
|
NE2
|
B:HIS400
|
3.5
|
31.2
|
1.0
|
|
O
|
B:HOH1502
|
3.5
|
45.9
|
1.0
|
|
ND1
|
B:HIS66
|
3.7
|
33.9
|
1.0
|
|
CG
|
B:HIS66
|
3.8
|
32.8
|
1.0
|
|
CD2
|
B:HIS400
|
3.8
|
30.1
|
1.0
|
|
CE1
|
B:HIS66
|
3.9
|
34.9
|
1.0
|
|
CG
|
B:HIS400
|
3.9
|
31.7
|
1.0
|
|
CU
|
B:CU502
|
3.9
|
50.4
|
1.0
|
|
CU
|
B:CU501
|
3.9
|
46.2
|
1.0
|
|
CA
|
B:HIS66
|
3.9
|
33.0
|
1.0
|
|
ND1
|
B:HIS64
|
4.0
|
38.0
|
1.0
|
|
CG
|
B:HIS64
|
4.0
|
36.9
|
1.0
|
|
CD2
|
B:HIS66
|
4.0
|
34.5
|
1.0
|
|
NE2
|
B:HIS66
|
4.1
|
34.9
|
1.0
|
|
CG
|
B:HIS398
|
4.1
|
38.2
|
1.0
|
|
ND1
|
B:HIS398
|
4.1
|
39.7
|
1.0
|
|
CB
|
B:HIS66
|
4.3
|
33.2
|
1.0
|
|
N
|
B:GLY67
|
4.3
|
32.2
|
1.0
|
|
C
|
B:HIS66
|
4.7
|
32.5
|
1.0
|
|
CA
|
B:HIS400
|
4.8
|
34.0
|
1.0
|
|
N
|
B:HIS66
|
4.8
|
32.5
|
1.0
|
|
CB
|
B:HIS400
|
4.8
|
33.7
|
1.0
|
|
O
|
B:LEU399
|
5.0
|
34.8
|
1.0
|
|
Copper binding site 9 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 9 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 9 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu500
b:45.9
occ:1.00
|
ND1
|
C:HIS458
|
2.1
|
44.5
|
1.0
|
|
SG
|
C:CYS453
|
2.3
|
39.6
|
1.0
|
|
ND1
|
C:HIS395
|
2.4
|
38.8
|
1.0
|
|
CE1
|
C:HIS458
|
3.1
|
44.7
|
1.0
|
|
CG
|
C:HIS458
|
3.1
|
43.5
|
1.0
|
|
CG
|
C:HIS395
|
3.3
|
37.9
|
1.0
|
|
CE1
|
C:HIS395
|
3.3
|
38.3
|
1.0
|
|
CB
|
C:CYS453
|
3.4
|
36.1
|
1.0
|
|
CB
|
C:HIS458
|
3.5
|
41.1
|
1.0
|
|
CB
|
C:HIS395
|
3.5
|
36.7
|
1.0
|
|
CD1
|
C:ILE455
|
3.6
|
34.6
|
1.0
|
|
CD2
|
C:PHE463
|
3.7
|
38.1
|
1.0
|
|
CB
|
C:ILE455
|
3.8
|
36.0
|
1.0
|
|
CE2
|
C:PHE463
|
3.8
|
37.8
|
1.0
|
|
CG1
|
C:ILE455
|
3.9
|
36.2
|
1.0
|
|
CA
|
C:HIS395
|
4.0
|
35.4
|
1.0
|
|
NE2
|
C:HIS458
|
4.2
|
46.0
|
1.0
|
|
CD2
|
C:HIS458
|
4.2
|
44.7
|
1.0
|
|
NE2
|
C:HIS395
|
4.4
|
40.3
|
1.0
|
|
CD2
|
C:HIS395
|
4.4
|
38.7
|
1.0
|
|
CG2
|
C:ILE455
|
4.6
|
35.0
|
1.0
|
|
CD
|
C:PRO396
|
4.6
|
34.7
|
1.0
|
|
CA
|
C:CYS453
|
4.8
|
35.8
|
1.0
|
|
O
|
C:GLY392
|
4.8
|
42.5
|
1.0
|
|
N
|
C:ILE455
|
4.8
|
35.8
|
1.0
|
|
CA
|
C:ILE455
|
4.9
|
35.8
|
1.0
|
|
C
|
C:HIS395
|
5.0
|
35.2
|
1.0
|
|
O
|
C:ILE455
|
5.0
|
36.0
|
1.0
|
|
CG
|
C:PHE463
|
5.0
|
37.1
|
1.0
|
|
CA
|
C:HIS458
|
5.0
|
40.2
|
1.0
|
|
Copper binding site 10 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 10 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 10 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu501
b:43.8
occ:1.00
|
O
|
C:HOH1492
|
1.9
|
35.0
|
1.0
|
|
NE2
|
C:HIS452
|
2.2
|
34.9
|
1.0
|
|
NE2
|
C:HIS400
|
2.2
|
30.9
|
1.0
|
|
NE2
|
C:HIS111
|
2.3
|
30.4
|
1.0
|
|
CE1
|
C:HIS452
|
2.9
|
34.7
|
1.0
|
|
CE1
|
C:HIS400
|
3.0
|
28.7
|
1.0
|
|
CD2
|
C:HIS111
|
3.2
|
32.0
|
1.0
|
|
CD2
|
C:HIS400
|
3.3
|
30.2
|
1.0
|
|
CE1
|
C:HIS111
|
3.3
|
30.6
|
1.0
|
|
CD2
|
C:HIS452
|
3.4
|
35.5
|
1.0
|
|
CD2
|
C:HIS398
|
3.5
|
38.6
|
1.0
|
|
CU
|
C:CU502
|
3.9
|
47.6
|
1.0
|
|
CU
|
C:CU503
|
3.9
|
72.5
|
1.0
|
|
ND1
|
C:HIS452
|
4.1
|
34.4
|
1.0
|
|
ND1
|
C:HIS400
|
4.2
|
30.6
|
1.0
|
|
NE2
|
C:HIS398
|
4.2
|
41.5
|
1.0
|
|
CG
|
C:HIS400
|
4.4
|
31.4
|
1.0
|
|
CG
|
C:HIS111
|
4.4
|
32.2
|
1.0
|
|
CG
|
C:HIS452
|
4.4
|
35.5
|
1.0
|
|
ND1
|
C:HIS111
|
4.4
|
31.2
|
1.0
|
|
CD2
|
C:HIS64
|
4.4
|
38.2
|
1.0
|
|
NE2
|
C:HIS454
|
4.7
|
31.1
|
1.0
|
|
CG
|
C:HIS398
|
4.7
|
38.9
|
1.0
|
|
CD2
|
C:HIS454
|
4.7
|
31.8
|
1.0
|
|
NE2
|
C:HIS64
|
4.7
|
39.3
|
1.0
|
|
CD2
|
C:PHE450
|
4.9
|
33.8
|
1.0
|
|
CG
|
C:HIS64
|
5.0
|
37.0
|
1.0
|
|
Copper binding site 11 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 11 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 11 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu502
b:47.6
occ:1.00
|
O
|
C:HOH1492
|
2.1
|
35.0
|
1.0
|
|
ND1
|
C:HIS66
|
2.3
|
35.4
|
1.0
|
|
NE2
|
C:HIS454
|
2.3
|
31.1
|
1.0
|
|
NE2
|
C:HIS109
|
2.4
|
30.9
|
1.0
|
|
CE1
|
C:HIS66
|
3.0
|
35.7
|
1.0
|
|
CD2
|
C:HIS454
|
3.2
|
31.8
|
1.0
|
|
CE1
|
C:HIS109
|
3.2
|
30.2
|
1.0
|
|
CG
|
C:HIS66
|
3.4
|
34.4
|
1.0
|
|
CE1
|
C:HIS454
|
3.4
|
31.0
|
1.0
|
|
CD2
|
C:HIS109
|
3.5
|
29.7
|
1.0
|
|
CD2
|
C:HIS64
|
3.7
|
38.2
|
1.0
|
|
CU
|
C:CU503
|
3.8
|
72.5
|
1.0
|
|
CB
|
C:HIS66
|
3.8
|
32.9
|
1.0
|
|
CU
|
C:CU501
|
3.9
|
43.8
|
1.0
|
|
CZ2
|
C:TRP107
|
4.0
|
30.4
|
1.0
|
|
CD2
|
C:HIS398
|
4.1
|
38.6
|
1.0
|
|
NE2
|
C:HIS66
|
4.1
|
34.9
|
1.0
|
|
NE2
|
C:HIS398
|
4.3
|
41.5
|
1.0
|
|
NE2
|
C:HIS64
|
4.3
|
39.3
|
1.0
|
|
CD2
|
C:HIS66
|
4.4
|
35.3
|
1.0
|
|
CG
|
C:HIS454
|
4.4
|
33.0
|
1.0
|
|
ND1
|
C:HIS109
|
4.4
|
31.1
|
1.0
|
|
ND1
|
C:HIS454
|
4.4
|
32.3
|
1.0
|
|
CE2
|
C:TRP107
|
4.5
|
30.1
|
1.0
|
|
CG
|
C:HIS109
|
4.6
|
30.2
|
1.0
|
|
CH2
|
C:TRP107
|
4.6
|
27.6
|
1.0
|
|
CB
|
C:ALA241
|
4.6
|
28.3
|
1.0
|
|
NE1
|
C:TRP107
|
4.7
|
28.5
|
1.0
|
|
CA
|
C:HIS66
|
4.7
|
32.4
|
1.0
|
|
CG
|
C:HIS64
|
4.8
|
37.0
|
1.0
|
|
CD2
|
C:HIS111
|
4.9
|
32.0
|
1.0
|
|
Copper binding site 12 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 12 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 12 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu503
b:72.5
occ:1.00
|
NE2
|
C:HIS398
|
2.0
|
41.5
|
1.0
|
|
NE2
|
C:HIS64
|
2.0
|
39.3
|
1.0
|
|
O
|
C:HOH1748
|
2.3
|
73.8
|
1.0
|
|
CD2
|
C:HIS64
|
2.9
|
38.2
|
1.0
|
|
CD2
|
C:HIS398
|
3.0
|
38.6
|
1.0
|
|
CE1
|
C:HIS64
|
3.0
|
36.9
|
1.0
|
|
CE1
|
C:HIS398
|
3.1
|
40.0
|
1.0
|
|
CE1
|
C:HIS400
|
3.2
|
28.7
|
1.0
|
|
NE2
|
C:HIS400
|
3.4
|
30.9
|
1.0
|
|
ND1
|
C:HIS400
|
3.4
|
30.6
|
1.0
|
|
O
|
C:HOH1492
|
3.5
|
35.0
|
1.0
|
|
ND1
|
C:HIS66
|
3.8
|
35.4
|
1.0
|
|
CD2
|
C:HIS400
|
3.8
|
30.2
|
1.0
|
|
CG
|
C:HIS400
|
3.8
|
31.4
|
1.0
|
|
CU
|
C:CU502
|
3.8
|
47.6
|
1.0
|
|
CG
|
C:HIS66
|
3.9
|
34.4
|
1.0
|
|
CU
|
C:CU501
|
3.9
|
43.8
|
1.0
|
|
CE1
|
C:HIS66
|
4.0
|
35.7
|
1.0
|
|
ND1
|
C:HIS64
|
4.0
|
37.6
|
1.0
|
|
CA
|
C:HIS66
|
4.0
|
32.4
|
1.0
|
|
CG
|
C:HIS64
|
4.0
|
37.0
|
1.0
|
|
CD2
|
C:HIS66
|
4.1
|
35.3
|
1.0
|
|
CG
|
C:HIS398
|
4.1
|
38.9
|
1.0
|
|
ND1
|
C:HIS398
|
4.1
|
40.1
|
1.0
|
|
NE2
|
C:HIS66
|
4.2
|
34.9
|
1.0
|
|
N
|
C:GLY67
|
4.3
|
33.7
|
1.0
|
|
CB
|
C:HIS66
|
4.3
|
32.9
|
1.0
|
|
C
|
C:HIS66
|
4.7
|
32.6
|
1.0
|
|
CA
|
C:HIS400
|
4.7
|
33.8
|
1.0
|
|
CB
|
C:HIS400
|
4.8
|
32.4
|
1.0
|
|
N
|
C:HIS66
|
4.8
|
32.8
|
1.0
|
|
O
|
C:LEU399
|
4.9
|
34.9
|
1.0
|
|
Copper binding site 13 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 13 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 13 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu500
b:47.6
occ:1.00
|
ND1
|
D:HIS458
|
2.2
|
45.2
|
1.0
|
|
SG
|
D:CYS453
|
2.2
|
39.1
|
1.0
|
|
ND1
|
D:HIS395
|
2.3
|
38.7
|
1.0
|
|
CE1
|
D:HIS458
|
3.1
|
45.8
|
1.0
|
|
CG
|
D:HIS395
|
3.2
|
37.4
|
1.0
|
|
CG
|
D:HIS458
|
3.2
|
43.1
|
1.0
|
|
CE1
|
D:HIS395
|
3.3
|
38.7
|
1.0
|
|
CB
|
D:CYS453
|
3.4
|
36.8
|
1.0
|
|
CD1
|
D:ILE455
|
3.4
|
34.6
|
1.0
|
|
CB
|
D:HIS395
|
3.4
|
35.7
|
1.0
|
|
CB
|
D:HIS458
|
3.5
|
41.2
|
1.0
|
|
CD2
|
D:PHE463
|
3.7
|
37.4
|
1.0
|
|
CB
|
D:ILE455
|
3.8
|
36.4
|
1.0
|
|
CE2
|
D:PHE463
|
3.8
|
37.9
|
1.0
|
|
CG1
|
D:ILE455
|
3.9
|
36.0
|
1.0
|
|
CA
|
D:HIS395
|
3.9
|
35.8
|
1.0
|
|
NE2
|
D:HIS458
|
4.3
|
45.7
|
1.0
|
|
CD2
|
D:HIS458
|
4.3
|
44.8
|
1.0
|
|
CD2
|
D:HIS395
|
4.4
|
38.5
|
1.0
|
|
NE2
|
D:HIS395
|
4.4
|
39.6
|
1.0
|
|
CD
|
D:PRO396
|
4.5
|
34.7
|
1.0
|
|
CG2
|
D:ILE455
|
4.6
|
36.1
|
1.0
|
|
CA
|
D:CYS453
|
4.7
|
35.5
|
1.0
|
|
N
|
D:ILE455
|
4.8
|
36.4
|
1.0
|
|
O
|
D:GLY392
|
4.8
|
42.0
|
1.0
|
|
C
|
D:HIS395
|
4.8
|
35.3
|
1.0
|
|
CA
|
D:ILE455
|
4.9
|
36.7
|
1.0
|
|
O
|
D:ILE455
|
4.9
|
34.8
|
1.0
|
|
N
|
D:HIS395
|
5.0
|
35.0
|
1.0
|
|
CG
|
D:PHE463
|
5.0
|
37.9
|
1.0
|
|
Copper binding site 14 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 14 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 14 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu501
b:44.5
occ:1.00
|
O
|
D:HOH1503
|
2.0
|
39.6
|
1.0
|
|
NE2
|
D:HIS400
|
2.2
|
30.2
|
1.0
|
|
NE2
|
D:HIS452
|
2.2
|
34.6
|
1.0
|
|
NE2
|
D:HIS111
|
2.3
|
29.6
|
1.0
|
|
CE1
|
D:HIS452
|
2.9
|
34.6
|
1.0
|
|
CE1
|
D:HIS400
|
3.0
|
28.0
|
1.0
|
|
CD2
|
D:HIS111
|
3.2
|
30.5
|
1.0
|
|
CD2
|
D:HIS400
|
3.3
|
29.9
|
1.0
|
|
CE1
|
D:HIS111
|
3.4
|
30.4
|
1.0
|
|
CD2
|
D:HIS452
|
3.4
|
34.7
|
1.0
|
|
CD2
|
D:HIS398
|
3.5
|
38.0
|
1.0
|
|
CU
|
D:CU502
|
3.9
|
47.7
|
1.0
|
|
CU
|
D:CU503
|
3.9
|
75.2
|
1.0
|
|
ND1
|
D:HIS452
|
4.1
|
34.6
|
1.0
|
|
ND1
|
D:HIS400
|
4.1
|
29.3
|
1.0
|
|
NE2
|
D:HIS398
|
4.1
|
40.0
|
1.0
|
|
CG
|
D:HIS400
|
4.3
|
31.1
|
1.0
|
|
CG
|
D:HIS452
|
4.4
|
34.9
|
1.0
|
|
CG
|
D:HIS111
|
4.4
|
31.2
|
1.0
|
|
CD2
|
D:HIS64
|
4.4
|
36.6
|
1.0
|
|
ND1
|
D:HIS111
|
4.5
|
30.1
|
1.0
|
|
CG
|
D:HIS398
|
4.6
|
38.4
|
1.0
|
|
NE2
|
D:HIS64
|
4.7
|
38.3
|
1.0
|
|
NE2
|
D:HIS454
|
4.7
|
31.1
|
1.0
|
|
CD2
|
D:HIS454
|
4.7
|
30.9
|
1.0
|
|
CD2
|
D:PHE450
|
4.9
|
34.0
|
1.0
|
|
CG
|
D:HIS64
|
4.9
|
36.1
|
1.0
|
|
Copper binding site 15 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 15 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 15 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu502
b:47.7
occ:1.00
|
O
|
D:HOH1503
|
2.0
|
39.6
|
1.0
|
|
ND1
|
D:HIS66
|
2.1
|
35.2
|
1.0
|
|
NE2
|
D:HIS454
|
2.3
|
31.1
|
1.0
|
|
NE2
|
D:HIS109
|
2.5
|
29.5
|
1.0
|
|
CE1
|
D:HIS66
|
2.8
|
36.2
|
1.0
|
|
CD2
|
D:HIS454
|
3.1
|
30.9
|
1.0
|
|
CG
|
D:HIS66
|
3.3
|
34.1
|
1.0
|
|
CE1
|
D:HIS109
|
3.3
|
29.2
|
1.0
|
|
CE1
|
D:HIS454
|
3.3
|
30.5
|
1.0
|
|
CD2
|
D:HIS109
|
3.6
|
28.6
|
1.0
|
|
CU
|
D:CU503
|
3.7
|
75.2
|
1.0
|
|
CD2
|
D:HIS64
|
3.7
|
36.6
|
1.0
|
|
CB
|
D:HIS66
|
3.9
|
33.0
|
1.0
|
|
CU
|
D:CU501
|
3.9
|
44.5
|
1.0
|
|
NE2
|
D:HIS66
|
4.0
|
35.3
|
1.0
|
|
CD2
|
D:HIS398
|
4.0
|
38.0
|
1.0
|
|
CZ2
|
D:TRP107
|
4.1
|
29.1
|
1.0
|
|
NE2
|
D:HIS398
|
4.2
|
40.0
|
1.0
|
|
CD2
|
D:HIS66
|
4.3
|
35.5
|
1.0
|
|
NE2
|
D:HIS64
|
4.3
|
38.3
|
1.0
|
|
CG
|
D:HIS454
|
4.3
|
32.7
|
1.0
|
|
ND1
|
D:HIS454
|
4.4
|
32.0
|
1.0
|
|
CE2
|
D:TRP107
|
4.5
|
28.7
|
1.0
|
|
ND1
|
D:HIS109
|
4.5
|
30.5
|
1.0
|
|
CB
|
D:ALA241
|
4.5
|
27.5
|
1.0
|
|
NE1
|
D:TRP107
|
4.7
|
27.7
|
1.0
|
|
CG
|
D:HIS109
|
4.7
|
30.0
|
1.0
|
|
CH2
|
D:TRP107
|
4.7
|
28.4
|
1.0
|
|
CA
|
D:HIS66
|
4.7
|
32.5
|
1.0
|
|
CG
|
D:HIS64
|
4.9
|
36.1
|
1.0
|
|
CG
|
D:HIS398
|
4.9
|
38.4
|
1.0
|
|
CD2
|
D:HIS111
|
5.0
|
30.5
|
1.0
|
|
Copper binding site 16 out
of 16 in 1kya
Go back to
Copper Binding Sites List in 1kya
Copper binding site 16 out
of 16 in the Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 16 of Active Laccase From Trametes Versicolor Complexed with 2,5-Xylidine within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu503
b:75.2
occ:1.00
|
NE2
|
D:HIS398
|
2.0
|
40.0
|
1.0
|
|
NE2
|
D:HIS64
|
2.0
|
38.3
|
1.0
|
|
O
|
D:HOH1747
|
2.9
|
77.8
|
1.0
|
|
CD2
|
D:HIS64
|
2.9
|
36.6
|
1.0
|
|
CE1
|
D:HIS64
|
3.0
|
36.9
|
1.0
|
|
CD2
|
D:HIS398
|
3.0
|
38.0
|
1.0
|
|
CE1
|
D:HIS398
|
3.0
|
39.7
|
1.0
|
|
O
|
D:HOH1503
|
3.2
|
39.6
|
1.0
|
|
CE1
|
D:HIS400
|
3.3
|
28.0
|
1.0
|
|
NE2
|
D:HIS400
|
3.5
|
30.2
|
1.0
|
|
ND1
|
D:HIS400
|
3.6
|
29.3
|
1.0
|
|
ND1
|
D:HIS66
|
3.6
|
35.2
|
1.0
|
|
CG
|
D:HIS66
|
3.7
|
34.1
|
1.0
|
|
CU
|
D:CU502
|
3.7
|
47.7
|
1.0
|
|
CE1
|
D:HIS66
|
3.8
|
36.2
|
1.0
|
|
CA
|
D:HIS66
|
3.8
|
32.5
|
1.0
|
|
CD2
|
D:HIS400
|
3.9
|
29.9
|
1.0
|
|
CG
|
D:HIS400
|
3.9
|
31.1
|
1.0
|
|
CU
|
D:CU501
|
3.9
|
44.5
|
1.0
|
|
CD2
|
D:HIS66
|
4.0
|
35.5
|
1.0
|
|
ND1
|
D:HIS64
|
4.0
|
36.4
|
1.0
|
|
CG
|
D:HIS64
|
4.0
|
36.1
|
1.0
|
|
NE2
|
D:HIS66
|
4.0
|
35.3
|
1.0
|
|
ND1
|
D:HIS398
|
4.1
|
39.2
|
1.0
|
|
CG
|
D:HIS398
|
4.1
|
38.4
|
1.0
|
|
N
|
D:GLY67
|
4.2
|
33.2
|
1.0
|
|
CB
|
D:HIS66
|
4.2
|
33.0
|
1.0
|
|
C
|
D:HIS66
|
4.6
|
33.0
|
1.0
|
|
N
|
D:HIS66
|
4.7
|
32.3
|
1.0
|
|
CA
|
D:HIS400
|
4.8
|
33.6
|
1.0
|
|
CB
|
D:HIS400
|
4.9
|
33.1
|
1.0
|
|
O
|
D:LEU399
|
5.0
|
34.2
|
1.0
|
|
Reference:
T.Bertrand,
C.Jolivalt,
P.Briozzo,
E.Caminade,
N.Joly,
C.Madzak,
C.Mougin.
Crystal Structure of A Four-Copper Laccase Complexed with An Arylamine: Insights Into Substrate Recognition and Correlation with Kinetics. Biochemistry V. 41 7325 2002.
ISSN: ISSN 0006-2960
PubMed: 12044164
DOI: 10.1021/BI0201318
Page generated: Wed Oct 28 14:15:29 2020
|
