Copper in PDB 5anh: Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
Enzymatic activity of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
All present enzymatic activity of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971):
1.10.3.2;
Protein crystallography data
The structure of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971), PDB code: 5anh
was solved by
F.J.Medrano,
A.Romero,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
49.180 /
2.49
|
|
Space group
|
C 1 2 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
101.440,
175.660,
103.700,
90.00,
104.16,
90.00
|
|
R / Rfree (%)
|
19.25 /
27.29
|
Copper Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Copper atom in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
(pdb code 5anh). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 12 binding sites of Copper where determined in the
Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971), PDB code: 5anh:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Copper binding site 1 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 1 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:46.6
occ:1.00
|
NE2
|
A:HIS64
|
2.1
|
21.0
|
1.0
|
|
NE2
|
A:HIS397
|
2.2
|
43.4
|
1.0
|
|
CE1
|
A:HIS397
|
2.7
|
36.0
|
1.0
|
|
CE1
|
A:HIS64
|
3.0
|
11.9
|
1.0
|
|
CD2
|
A:HIS64
|
3.1
|
14.9
|
1.0
|
|
ND1
|
A:HIS66
|
3.4
|
16.5
|
1.0
|
|
CD2
|
A:HIS397
|
3.4
|
34.5
|
1.0
|
|
CG
|
A:HIS66
|
3.6
|
14.7
|
1.0
|
|
CE1
|
A:HIS66
|
3.7
|
19.7
|
1.0
|
|
NE2
|
A:HIS399
|
3.7
|
28.4
|
1.0
|
|
CE1
|
A:HIS399
|
3.7
|
27.5
|
1.0
|
|
CD2
|
A:HIS399
|
3.8
|
21.3
|
1.0
|
|
ND1
|
A:HIS399
|
3.8
|
24.0
|
1.0
|
|
CA
|
A:HIS66
|
3.8
|
27.2
|
1.0
|
|
N
|
A:GLY67
|
3.8
|
32.1
|
1.0
|
|
CG
|
A:HIS399
|
3.8
|
22.9
|
1.0
|
|
ND1
|
A:HIS397
|
4.0
|
26.2
|
1.0
|
|
CD2
|
A:HIS66
|
4.0
|
17.5
|
1.0
|
|
CU
|
A:CU603
|
4.0
|
38.4
|
1.0
|
|
NE2
|
A:HIS66
|
4.0
|
15.5
|
1.0
|
|
CB
|
A:HIS66
|
4.1
|
11.0
|
1.0
|
|
ND1
|
A:HIS64
|
4.1
|
20.9
|
1.0
|
|
CG
|
A:HIS64
|
4.2
|
19.3
|
1.0
|
|
C
|
A:HIS66
|
4.3
|
30.6
|
1.0
|
|
CG
|
A:HIS397
|
4.3
|
24.4
|
1.0
|
|
CA
|
A:HIS399
|
4.4
|
25.7
|
1.0
|
|
CU
|
A:CU602
|
4.5
|
34.8
|
1.0
|
|
CB
|
A:HIS399
|
4.6
|
27.6
|
1.0
|
|
O
|
A:HOH2033
|
4.6
|
20.5
|
1.0
|
|
CA
|
A:GLY67
|
4.8
|
17.7
|
1.0
|
|
N
|
A:HIS399
|
4.8
|
28.9
|
1.0
|
|
N
|
A:HIS66
|
4.9
|
24.4
|
1.0
|
|
Copper binding site 2 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 2 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:34.8
occ:1.00
|
NE2
|
A:HIS399
|
2.1
|
28.4
|
1.0
|
|
NE2
|
A:HIS111
|
2.1
|
26.1
|
1.0
|
|
NE2
|
A:HIS449
|
2.1
|
22.5
|
1.0
|
|
CE1
|
A:HIS399
|
2.8
|
27.5
|
1.0
|
|
CE1
|
A:HIS111
|
3.0
|
33.4
|
1.0
|
|
CE1
|
A:HIS449
|
3.1
|
27.1
|
1.0
|
|
CD2
|
A:HIS449
|
3.1
|
16.2
|
1.0
|
|
CD2
|
A:HIS111
|
3.1
|
26.8
|
1.0
|
|
CD2
|
A:HIS399
|
3.3
|
21.3
|
1.0
|
|
O
|
A:HOH2053
|
3.3
|
32.5
|
1.0
|
|
CD2
|
A:HIS397
|
3.8
|
34.5
|
1.0
|
|
ND1
|
A:HIS399
|
4.0
|
24.0
|
1.0
|
|
ND1
|
A:HIS111
|
4.2
|
37.0
|
1.0
|
|
NE2
|
A:HIS397
|
4.2
|
43.4
|
1.0
|
|
CD2
|
A:PHE447
|
4.2
|
37.0
|
1.0
|
|
ND1
|
A:HIS449
|
4.2
|
32.6
|
1.0
|
|
CG
|
A:HIS111
|
4.2
|
26.6
|
1.0
|
|
CG
|
A:HIS449
|
4.3
|
18.6
|
1.0
|
|
CG
|
A:HIS399
|
4.3
|
22.9
|
1.0
|
|
CB
|
A:PHE447
|
4.4
|
18.8
|
1.0
|
|
CU
|
A:CU601
|
4.5
|
46.6
|
1.0
|
|
CD2
|
A:HIS64
|
4.5
|
14.9
|
1.0
|
|
CG
|
A:PHE447
|
4.7
|
29.7
|
1.0
|
|
NE2
|
A:HIS64
|
4.8
|
21.0
|
1.0
|
|
CU
|
A:CU603
|
4.8
|
38.4
|
1.0
|
|
NE2
|
A:HIS451
|
4.8
|
35.9
|
1.0
|
|
CD2
|
A:HIS451
|
4.8
|
35.9
|
1.0
|
|
CG
|
A:PRO79
|
4.9
|
19.6
|
1.0
|
|
Copper binding site 3 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 3 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:38.4
occ:1.00
|
ND1
|
A:HIS66
|
1.8
|
16.5
|
1.0
|
|
NE2
|
A:HIS109
|
2.2
|
18.1
|
1.0
|
|
NE2
|
A:HIS451
|
2.2
|
35.9
|
1.0
|
|
CE1
|
A:HIS66
|
2.7
|
19.7
|
1.0
|
|
CG
|
A:HIS66
|
3.0
|
14.7
|
1.0
|
|
CE1
|
A:HIS451
|
3.1
|
34.5
|
1.0
|
|
CD2
|
A:HIS109
|
3.2
|
19.9
|
1.0
|
|
CE1
|
A:HIS109
|
3.2
|
11.8
|
1.0
|
|
CD2
|
A:HIS451
|
3.3
|
35.9
|
1.0
|
|
CB
|
A:HIS66
|
3.5
|
11.0
|
1.0
|
|
CZ2
|
A:TRP107
|
3.6
|
15.6
|
1.0
|
|
CD2
|
A:HIS64
|
3.8
|
14.9
|
1.0
|
|
NE2
|
A:HIS66
|
3.9
|
15.5
|
1.0
|
|
O
|
A:HOH2053
|
3.9
|
32.5
|
1.0
|
|
CU
|
A:CU601
|
4.0
|
46.6
|
1.0
|
|
CD2
|
A:HIS66
|
4.0
|
17.5
|
1.0
|
|
CE2
|
A:TRP107
|
4.0
|
16.9
|
1.0
|
|
NE2
|
A:HIS397
|
4.2
|
43.4
|
1.0
|
|
ND1
|
A:HIS451
|
4.2
|
27.7
|
1.0
|
|
NE1
|
A:TRP107
|
4.3
|
18.1
|
1.0
|
|
CH2
|
A:TRP107
|
4.3
|
27.0
|
1.0
|
|
NE2
|
A:HIS64
|
4.3
|
21.0
|
1.0
|
|
ND1
|
A:HIS109
|
4.3
|
23.5
|
1.0
|
|
CG
|
A:HIS109
|
4.3
|
24.3
|
1.0
|
|
CD2
|
A:HIS397
|
4.3
|
34.5
|
1.0
|
|
CG
|
A:HIS451
|
4.4
|
30.4
|
1.0
|
|
CB
|
A:ALA240
|
4.5
|
8.2
|
1.0
|
|
CA
|
A:HIS66
|
4.6
|
27.2
|
1.0
|
|
CU
|
A:CU602
|
4.8
|
34.8
|
1.0
|
|
CD2
|
A:TRP107
|
5.0
|
21.9
|
1.0
|
|
Copper binding site 4 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 4 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu604
b:27.7
occ:1.00
|
SG
|
A:CYS450
|
2.0
|
30.2
|
1.0
|
|
ND1
|
A:HIS455
|
2.1
|
33.2
|
1.0
|
|
CD2
|
A:HIS394
|
2.4
|
16.2
|
1.0
|
|
CG
|
A:HIS394
|
3.0
|
23.1
|
1.0
|
|
CE1
|
A:HIS455
|
3.0
|
28.8
|
1.0
|
|
CG
|
A:HIS455
|
3.1
|
32.0
|
1.0
|
|
CB
|
A:HIS394
|
3.3
|
16.2
|
1.0
|
|
CB
|
A:CYS450
|
3.3
|
22.3
|
1.0
|
|
CB
|
A:HIS455
|
3.4
|
22.0
|
1.0
|
|
NE2
|
A:HIS394
|
3.5
|
22.2
|
1.0
|
|
CD1
|
A:ILE452
|
3.5
|
20.5
|
1.0
|
|
CB
|
A:ILE452
|
3.7
|
30.7
|
1.0
|
|
CG1
|
A:ILE452
|
3.8
|
27.1
|
1.0
|
|
CD2
|
A:PHE460
|
3.8
|
22.3
|
1.0
|
|
CA
|
A:HIS394
|
3.9
|
36.8
|
1.0
|
|
CE2
|
A:PHE460
|
4.1
|
22.5
|
1.0
|
|
NE2
|
A:HIS455
|
4.1
|
29.9
|
1.0
|
|
CD2
|
A:HIS455
|
4.2
|
27.3
|
1.0
|
|
ND1
|
A:HIS394
|
4.2
|
31.6
|
1.0
|
|
CE1
|
A:HIS394
|
4.4
|
27.2
|
1.0
|
|
CG2
|
A:ILE452
|
4.5
|
29.7
|
1.0
|
|
CD
|
A:PRO395
|
4.5
|
18.8
|
1.0
|
|
CA
|
A:CYS450
|
4.7
|
24.7
|
1.0
|
|
N
|
A:ILE452
|
4.8
|
20.5
|
1.0
|
|
CA
|
A:ILE452
|
4.8
|
35.5
|
1.0
|
|
N
|
A:HIS394
|
4.8
|
35.1
|
1.0
|
|
O
|
A:ILE452
|
4.9
|
21.3
|
1.0
|
|
C
|
A:HIS394
|
4.9
|
36.3
|
1.0
|
|
O
|
A:GLY391
|
4.9
|
35.0
|
1.0
|
|
CA
|
A:HIS455
|
5.0
|
25.2
|
1.0
|
|
Copper binding site 5 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 5 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu601
b:44.8
occ:1.00
|
NE2
|
B:HIS397
|
2.1
|
29.6
|
1.0
|
|
NE2
|
B:HIS64
|
2.1
|
25.4
|
1.0
|
|
CE1
|
B:HIS397
|
2.7
|
36.0
|
1.0
|
|
CD2
|
B:HIS64
|
3.1
|
31.1
|
1.0
|
|
CE1
|
B:HIS64
|
3.2
|
28.8
|
1.0
|
|
CD2
|
B:HIS397
|
3.3
|
18.8
|
1.0
|
|
CG
|
B:HIS66
|
3.5
|
14.9
|
1.0
|
|
CE1
|
B:HIS399
|
3.6
|
29.4
|
1.0
|
|
CA
|
B:HIS66
|
3.6
|
21.5
|
1.0
|
|
ND1
|
B:HIS66
|
3.6
|
20.7
|
1.0
|
|
ND1
|
B:HIS399
|
3.7
|
22.4
|
1.0
|
|
NE2
|
B:HIS399
|
3.7
|
30.1
|
1.0
|
|
CD2
|
B:HIS66
|
3.8
|
23.7
|
1.0
|
|
N
|
B:GLY67
|
3.9
|
16.6
|
1.0
|
|
CG
|
B:HIS399
|
3.9
|
28.8
|
1.0
|
|
CD2
|
B:HIS399
|
3.9
|
31.3
|
1.0
|
|
CB
|
B:HIS66
|
3.9
|
23.1
|
1.0
|
|
ND1
|
B:HIS397
|
3.9
|
30.0
|
1.0
|
|
CE1
|
B:HIS66
|
3.9
|
22.1
|
1.0
|
|
CU
|
B:CU603
|
4.1
|
32.8
|
1.0
|
|
NE2
|
B:HIS66
|
4.1
|
25.4
|
1.0
|
|
C
|
B:HIS66
|
4.2
|
23.9
|
1.0
|
|
CG
|
B:HIS64
|
4.2
|
35.0
|
1.0
|
|
ND1
|
B:HIS64
|
4.2
|
40.1
|
1.0
|
|
CG
|
B:HIS397
|
4.3
|
21.6
|
1.0
|
|
CU
|
B:CU602
|
4.4
|
35.5
|
1.0
|
|
N
|
B:HIS66
|
4.5
|
24.2
|
1.0
|
|
CA
|
B:HIS399
|
4.6
|
41.5
|
1.0
|
|
O
|
B:HOH2153
|
4.6
|
27.0
|
1.0
|
|
CB
|
B:HIS399
|
4.7
|
40.2
|
1.0
|
|
CA
|
B:GLY67
|
5.0
|
16.4
|
1.0
|
|
Copper binding site 6 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 6 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu602
b:35.5
occ:1.00
|
NE2
|
B:HIS399
|
2.1
|
30.1
|
1.0
|
|
NE2
|
B:HIS449
|
2.1
|
37.7
|
1.0
|
|
NE2
|
B:HIS111
|
2.1
|
25.6
|
1.0
|
|
CE1
|
B:HIS449
|
2.8
|
32.1
|
1.0
|
|
CE1
|
B:HIS399
|
3.0
|
29.4
|
1.0
|
|
CD2
|
B:HIS111
|
3.0
|
24.8
|
1.0
|
|
CD2
|
B:HIS399
|
3.2
|
31.3
|
1.0
|
|
CE1
|
B:HIS111
|
3.2
|
30.1
|
1.0
|
|
CD2
|
B:HIS449
|
3.2
|
45.5
|
1.0
|
|
CD2
|
B:HIS397
|
3.6
|
18.8
|
1.0
|
|
NE2
|
B:HIS397
|
3.9
|
29.6
|
1.0
|
|
ND1
|
B:HIS449
|
4.0
|
35.9
|
1.0
|
|
ND1
|
B:HIS399
|
4.1
|
22.4
|
1.0
|
|
CG
|
B:HIS449
|
4.2
|
36.9
|
1.0
|
|
CG
|
B:HIS111
|
4.2
|
19.8
|
1.0
|
|
CG
|
B:HIS399
|
4.2
|
28.8
|
1.0
|
|
ND1
|
B:HIS111
|
4.3
|
26.9
|
1.0
|
|
CD2
|
B:PHE447
|
4.4
|
25.6
|
1.0
|
|
CU
|
B:CU601
|
4.4
|
44.8
|
1.0
|
|
O
|
B:HOH2162
|
4.4
|
38.9
|
1.0
|
|
CB
|
B:PHE447
|
4.4
|
21.3
|
1.0
|
|
CD2
|
B:HIS64
|
4.4
|
31.1
|
1.0
|
|
NE2
|
B:HIS451
|
4.5
|
23.6
|
1.0
|
|
CD2
|
B:HIS451
|
4.6
|
25.2
|
1.0
|
|
NE2
|
B:HIS64
|
4.6
|
25.4
|
1.0
|
|
CG
|
B:PHE447
|
4.8
|
25.6
|
1.0
|
|
CU
|
B:CU603
|
4.9
|
32.8
|
1.0
|
|
CG
|
B:HIS397
|
4.9
|
21.6
|
1.0
|
|
Copper binding site 7 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 7 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu603
b:32.8
occ:1.00
|
ND1
|
B:HIS66
|
1.8
|
20.7
|
1.0
|
|
NE2
|
B:HIS451
|
2.2
|
23.6
|
1.0
|
|
NE2
|
B:HIS109
|
2.3
|
19.7
|
1.0
|
|
CE1
|
B:HIS66
|
2.7
|
22.1
|
1.0
|
|
CG
|
B:HIS66
|
2.8
|
14.9
|
1.0
|
|
CE1
|
B:HIS451
|
3.0
|
21.2
|
1.0
|
|
CD2
|
B:HIS109
|
3.0
|
15.2
|
1.0
|
|
CB
|
B:HIS66
|
3.2
|
23.1
|
1.0
|
|
CD2
|
B:HIS451
|
3.3
|
25.2
|
1.0
|
|
CZ2
|
B:TRP107
|
3.4
|
14.7
|
1.0
|
|
CE1
|
B:HIS109
|
3.4
|
18.0
|
1.0
|
|
CE2
|
B:TRP107
|
3.8
|
14.1
|
1.0
|
|
NE2
|
B:HIS66
|
3.8
|
25.4
|
1.0
|
|
CD2
|
B:HIS66
|
3.9
|
23.7
|
1.0
|
|
CD2
|
B:HIS64
|
3.9
|
31.1
|
1.0
|
|
CH2
|
B:TRP107
|
4.0
|
16.0
|
1.0
|
|
CU
|
B:CU601
|
4.1
|
44.8
|
1.0
|
|
NE1
|
B:TRP107
|
4.1
|
13.7
|
1.0
|
|
ND1
|
B:HIS451
|
4.1
|
16.3
|
1.0
|
|
CG
|
B:HIS109
|
4.3
|
18.6
|
1.0
|
|
CG
|
B:HIS451
|
4.3
|
25.5
|
1.0
|
|
CA
|
B:HIS66
|
4.4
|
21.5
|
1.0
|
|
NE2
|
B:HIS397
|
4.4
|
29.6
|
1.0
|
|
ND1
|
B:HIS109
|
4.4
|
13.5
|
1.0
|
|
CD2
|
B:HIS397
|
4.5
|
18.8
|
1.0
|
|
NE2
|
B:HIS64
|
4.5
|
25.4
|
1.0
|
|
CB
|
B:ALA240
|
4.6
|
19.6
|
1.0
|
|
CD2
|
B:TRP107
|
4.7
|
18.1
|
1.0
|
|
CZ3
|
B:TRP107
|
4.8
|
16.4
|
1.0
|
|
CU
|
B:CU602
|
4.9
|
35.5
|
1.0
|
|
Copper binding site 8 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 8 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu604
b:30.4
occ:1.00
|
SG
|
B:CYS450
|
2.1
|
40.9
|
1.0
|
|
ND1
|
B:HIS455
|
2.2
|
19.9
|
1.0
|
|
ND1
|
B:HIS394
|
2.2
|
20.2
|
1.0
|
|
CG
|
B:HIS394
|
2.9
|
26.2
|
1.0
|
|
CB
|
B:HIS394
|
3.1
|
22.2
|
1.0
|
|
CE1
|
B:HIS455
|
3.1
|
24.7
|
1.0
|
|
CG
|
B:HIS455
|
3.2
|
30.6
|
1.0
|
|
CB
|
B:CYS450
|
3.2
|
26.4
|
1.0
|
|
CE1
|
B:HIS394
|
3.3
|
27.1
|
1.0
|
|
CB
|
B:HIS455
|
3.5
|
28.6
|
1.0
|
|
CD1
|
B:ILE452
|
3.6
|
17.3
|
1.0
|
|
CD2
|
B:PHE460
|
3.6
|
37.8
|
1.0
|
|
CA
|
B:HIS394
|
3.7
|
26.6
|
1.0
|
|
CB
|
B:ILE452
|
3.8
|
25.5
|
1.0
|
|
CE2
|
B:PHE460
|
3.9
|
35.0
|
1.0
|
|
CG1
|
B:ILE452
|
3.9
|
21.1
|
1.0
|
|
CD2
|
B:HIS394
|
4.1
|
34.6
|
1.0
|
|
NE2
|
B:HIS394
|
4.2
|
38.0
|
1.0
|
|
NE2
|
B:HIS455
|
4.2
|
29.9
|
1.0
|
|
CD2
|
B:HIS455
|
4.3
|
30.9
|
1.0
|
|
CG2
|
B:ILE452
|
4.5
|
18.3
|
1.0
|
|
CD
|
B:PRO395
|
4.5
|
33.1
|
1.0
|
|
CA
|
B:CYS450
|
4.6
|
27.3
|
1.0
|
|
O
|
B:GLY391
|
4.6
|
31.5
|
1.0
|
|
N
|
B:HIS394
|
4.7
|
31.0
|
1.0
|
|
C
|
B:HIS394
|
4.8
|
29.8
|
1.0
|
|
CG
|
B:PHE460
|
4.9
|
34.4
|
1.0
|
|
N
|
B:ILE452
|
4.9
|
26.4
|
1.0
|
|
CA
|
B:ILE452
|
4.9
|
35.1
|
1.0
|
|
CE2
|
B:PHE336
|
5.0
|
33.6
|
1.0
|
|
Copper binding site 9 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 9 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 9 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu601
b:48.4
occ:1.00
|
NE2
|
C:HIS64
|
2.0
|
12.5
|
1.0
|
|
NE2
|
C:HIS397
|
2.0
|
30.0
|
1.0
|
|
CE1
|
C:HIS397
|
2.8
|
27.8
|
1.0
|
|
CE1
|
C:HIS64
|
2.9
|
20.9
|
1.0
|
|
CD2
|
C:HIS64
|
3.1
|
12.5
|
1.0
|
|
CD2
|
C:HIS397
|
3.2
|
30.2
|
1.0
|
|
CG
|
C:HIS66
|
3.5
|
18.0
|
1.0
|
|
NE2
|
C:HIS399
|
3.6
|
24.9
|
1.0
|
|
CA
|
C:HIS66
|
3.6
|
20.1
|
1.0
|
|
CE1
|
C:HIS399
|
3.6
|
25.5
|
1.0
|
|
N
|
C:GLY67
|
3.7
|
25.7
|
1.0
|
|
CD2
|
C:HIS66
|
3.7
|
20.6
|
1.0
|
|
ND1
|
C:HIS399
|
3.7
|
28.4
|
1.0
|
|
CD2
|
C:HIS399
|
3.7
|
15.5
|
1.0
|
|
ND1
|
C:HIS66
|
3.8
|
23.8
|
1.0
|
|
CG
|
C:HIS399
|
3.9
|
22.7
|
1.0
|
|
CB
|
C:HIS66
|
3.9
|
16.9
|
1.0
|
|
ND1
|
C:HIS397
|
4.0
|
35.3
|
1.0
|
|
ND1
|
C:HIS64
|
4.0
|
26.0
|
1.0
|
|
NE2
|
C:HIS66
|
4.1
|
25.4
|
1.0
|
|
CE1
|
C:HIS66
|
4.1
|
27.8
|
1.0
|
|
C
|
C:HIS66
|
4.1
|
21.4
|
1.0
|
|
CG
|
C:HIS64
|
4.1
|
26.1
|
1.0
|
|
CG
|
C:HIS397
|
4.2
|
32.1
|
1.0
|
|
CU
|
C:CU603
|
4.2
|
33.7
|
1.0
|
|
CA
|
C:HIS399
|
4.4
|
16.0
|
1.0
|
|
O
|
C:HOH2156
|
4.4
|
25.3
|
1.0
|
|
CU
|
C:CU602
|
4.5
|
43.4
|
1.0
|
|
N
|
C:HIS66
|
4.6
|
21.5
|
1.0
|
|
CB
|
C:HIS399
|
4.7
|
18.9
|
1.0
|
|
CA
|
C:GLY67
|
4.7
|
25.4
|
1.0
|
|
N
|
C:HIS399
|
4.8
|
26.6
|
1.0
|
|
Copper binding site 10 out
of 12 in 5anh
Go back to
Copper Binding Sites List in 5anh
Copper binding site 10 out
of 12 in the Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971)
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 10 of Crystal Structure of Laccase From Basidiomycete PM1 (Cect 2971) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu602
b:43.4
occ:1.00
|
NE2
|
C:HIS399
|
2.0
|
24.9
|
1.0
|
|
NE2
|
C:HIS111
|
2.1
|
23.6
|
1.0
|
|
NE2
|
C:HIS449
|
2.2
|
31.4
|
1.0
|
|
CE1
|
C:HIS399
|
2.9
|
25.5
|
1.0
|
|
CE1
|
C:HIS111
|
2.9
|
19.8
|
1.0
|
|
CD2
|
C:HIS399
|
3.1
|
15.5
|
1.0
|
|
CE1
|
C:HIS449
|
3.1
|
28.2
|
1.0
|
|
CD2
|
C:HIS111
|
3.3
|
16.2
|
1.0
|
|
CD2
|
C:HIS449
|
3.3
|
38.1
|
1.0
|
|
CD2
|
C:HIS397
|
3.9
|
30.2
|
1.0
|
|
ND1
|
C:HIS399
|
4.1
|
28.4
|
1.0
|
|
CD2
|
C:PHE447
|
4.1
|
35.9
|
1.0
|
|
ND1
|
C:HIS111
|
4.1
|
22.9
|
1.0
|
|
CG
|
C:HIS399
|
4.2
|
22.7
|
1.0
|
|
ND1
|
C:HIS449
|
4.3
|
26.9
|
1.0
|
|
CG
|
C:HIS111
|
4.3
|
17.9
|
1.0
|
|
CB
|
C:PHE447
|
4.3
|
29.5
|
1.0
|
|
CG
|
C:HIS449
|
4.4
|
30.2
|
1.0
|
|
NE2
|
C:HIS397
|
4.4
|
30.0
|
1.0
|
|
CD2
|
C:HIS64
|
4.5
|
12.5
|
1.0
|
|
CU
|
C:CU601
|
4.5
|
48.4
|
1.0
|
|
CG
|
C:PHE447
|
4.7
|
38.5
|
1.0
|
|
NE2
|
C:HIS64
|
4.7
|
12.5
|
1.0
|
|
CG
|
C:PRO79
|
4.8
|
16.4
|
1.0
|
|
CU
|
C:CU603
|
4.9
|
33.7
|
1.0
|
|
NE2
|
C:HIS451
|
4.9
|
24.2
|
1.0
|
|
Reference:
I.Pardo,
G.Santiago,
P.Gentili,
F.Lucas,
E.Monza,
F.J.Medrano,
A.Romero,
C.Galli,
A.T.Martinez,
V.Guallar,
S.Camarero.
Re-Designing the Substrate Binding Pocket of Laccase For Enhanced Oxidation of Sinapic Acid Catal.Sci..Technol V. 6 3900 2016.
ISSN: ISSN 2044-4753
DOI: 10.1039/C5CY01725D
Page generated: Sun Dec 13 11:17:00 2020
|
