Copper in PDB 3t6v: Crystal Structure of Laccase From Steccherinum Ochraceum
Protein crystallography data
The structure of Crystal Structure of Laccase From Steccherinum Ochraceum, PDB code: 3t6v
was solved by
M.Ferraroni,
F.Briganti,
I.Matera,
M.Kolomytseva,
L.Golovleva,
A.Scozzafava,
A.M.Chernykh,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
73.535,
140.662,
174.178,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.1 /
24.1
|
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 Steccherinum Ochraceum
(pdb code 3t6v). 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 Steccherinum Ochraceum, PDB code: 3t6v:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Copper binding site 1 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 1 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:19.7
occ:1.00
|
ND1
|
A:HIS397
|
2.1
|
14.7
|
1.0
|
ND1
|
A:HIS458
|
2.1
|
15.4
|
1.0
|
SG
|
A:CYS453
|
2.1
|
19.8
|
1.0
|
CE1
|
A:HIS397
|
3.0
|
13.3
|
1.0
|
CE1
|
A:HIS458
|
3.1
|
15.3
|
1.0
|
CG
|
A:HIS458
|
3.1
|
16.1
|
1.0
|
CG
|
A:HIS397
|
3.1
|
15.2
|
1.0
|
CB
|
A:CYS453
|
3.3
|
16.1
|
1.0
|
CB
|
A:HIS458
|
3.4
|
18.1
|
1.0
|
CB
|
A:HIS397
|
3.5
|
15.3
|
1.0
|
CD1
|
A:ILE455
|
3.6
|
11.2
|
1.0
|
CD2
|
A:PHE463
|
3.8
|
20.4
|
1.0
|
CB
|
A:ILE455
|
3.9
|
13.1
|
1.0
|
CA
|
A:HIS397
|
4.0
|
16.5
|
1.0
|
CE2
|
A:PHE463
|
4.1
|
19.9
|
1.0
|
CG1
|
A:ILE455
|
4.1
|
13.5
|
1.0
|
NE2
|
A:HIS397
|
4.2
|
19.6
|
1.0
|
NE2
|
A:HIS458
|
4.2
|
18.3
|
1.0
|
CD2
|
A:HIS458
|
4.2
|
14.3
|
1.0
|
CD2
|
A:HIS397
|
4.2
|
15.4
|
1.0
|
CA
|
A:CYS453
|
4.7
|
15.8
|
1.0
|
N
|
A:ILE455
|
4.7
|
14.4
|
1.0
|
CD
|
A:PRO398
|
4.7
|
12.5
|
1.0
|
CA
|
A:ILE455
|
4.8
|
13.9
|
1.0
|
CG2
|
A:ILE455
|
4.8
|
11.7
|
1.0
|
O
|
A:ILE455
|
4.9
|
14.4
|
1.0
|
CA
|
A:HIS458
|
4.9
|
17.9
|
1.0
|
CE1
|
A:PHE341
|
5.0
|
18.9
|
1.0
|
CZ
|
A:PHE341
|
5.0
|
15.8
|
1.0
|
C
|
A:HIS397
|
5.0
|
14.5
|
1.0
|
N
|
A:HIS397
|
5.0
|
15.8
|
1.0
|
|
Copper binding site 2 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 2 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:15.8
occ:1.00
|
ND1
|
A:HIS67
|
2.0
|
10.3
|
1.0
|
NE2
|
A:HIS110
|
2.1
|
11.4
|
1.0
|
NE2
|
A:HIS454
|
2.1
|
10.8
|
1.0
|
O
|
A:HOH944
|
2.8
|
15.0
|
0.5
|
CE1
|
A:HIS110
|
2.9
|
11.7
|
1.0
|
CE1
|
A:HIS67
|
3.0
|
9.0
|
1.0
|
CG
|
A:HIS67
|
3.0
|
11.5
|
1.0
|
CE1
|
A:HIS454
|
3.0
|
6.3
|
1.0
|
CD2
|
A:HIS110
|
3.1
|
14.7
|
1.0
|
CD2
|
A:HIS454
|
3.1
|
11.3
|
1.0
|
CB
|
A:HIS67
|
3.4
|
11.8
|
1.0
|
CZ2
|
A:TRP108
|
3.7
|
9.2
|
1.0
|
CD2
|
A:HIS65
|
3.9
|
14.8
|
1.0
|
CE2
|
A:TRP108
|
3.9
|
8.6
|
1.0
|
NE1
|
A:TRP108
|
4.0
|
9.0
|
1.0
|
CU
|
A:CU504
|
4.1
|
18.1
|
1.0
|
NE2
|
A:HIS67
|
4.1
|
12.3
|
1.0
|
ND1
|
A:HIS110
|
4.1
|
13.0
|
1.0
|
CD2
|
A:HIS67
|
4.1
|
10.7
|
1.0
|
ND1
|
A:HIS454
|
4.2
|
7.8
|
1.0
|
CG
|
A:HIS110
|
4.2
|
12.3
|
1.0
|
CG
|
A:HIS454
|
4.3
|
14.0
|
1.0
|
CB
|
A:ALA244
|
4.3
|
10.6
|
1.0
|
NE2
|
A:HIS65
|
4.4
|
13.9
|
1.0
|
CA
|
A:HIS67
|
4.4
|
12.0
|
1.0
|
NE2
|
A:HIS400
|
4.4
|
12.3
|
1.0
|
CD2
|
A:HIS400
|
4.4
|
7.0
|
1.0
|
CH2
|
A:TRP108
|
4.5
|
12.4
|
1.0
|
O
|
A:HOH723
|
4.5
|
22.8
|
1.0
|
CD2
|
A:TRP108
|
4.9
|
8.1
|
1.0
|
|
Copper binding site 3 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 3 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:19.3
occ:1.00
|
NE2
|
A:HIS452
|
2.0
|
15.7
|
1.0
|
NE2
|
A:HIS402
|
2.0
|
13.2
|
1.0
|
NE2
|
A:HIS112
|
2.2
|
13.1
|
1.0
|
O
|
A:HOH944
|
2.5
|
15.0
|
0.5
|
CE1
|
A:HIS402
|
2.9
|
18.2
|
1.0
|
CD2
|
A:HIS452
|
3.0
|
14.9
|
1.0
|
CE1
|
A:HIS452
|
3.0
|
17.0
|
1.0
|
CD2
|
A:HIS112
|
3.1
|
10.8
|
1.0
|
CD2
|
A:HIS402
|
3.1
|
13.7
|
1.0
|
CE1
|
A:HIS112
|
3.2
|
15.3
|
1.0
|
O
|
A:HOH723
|
3.8
|
22.8
|
1.0
|
CD2
|
A:PHE450
|
3.9
|
15.0
|
1.0
|
ND1
|
A:HIS402
|
4.1
|
14.7
|
1.0
|
CD2
|
A:HIS400
|
4.1
|
7.0
|
1.0
|
ND1
|
A:HIS452
|
4.1
|
17.9
|
1.0
|
CG
|
A:HIS452
|
4.2
|
13.2
|
1.0
|
CG
|
A:HIS402
|
4.2
|
15.9
|
1.0
|
CG
|
A:HIS112
|
4.3
|
15.7
|
1.0
|
ND1
|
A:HIS112
|
4.3
|
14.4
|
1.0
|
CU
|
A:CU504
|
4.3
|
18.1
|
1.0
|
CB
|
A:PHE450
|
4.4
|
15.3
|
1.0
|
CD2
|
A:HIS65
|
4.4
|
14.8
|
1.0
|
NE2
|
A:HIS65
|
4.5
|
13.9
|
1.0
|
CG
|
A:PHE450
|
4.6
|
18.9
|
1.0
|
NE2
|
A:HIS400
|
4.7
|
12.3
|
1.0
|
CE2
|
A:PHE450
|
4.7
|
16.1
|
1.0
|
|
Copper binding site 4 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 4 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu504
b:18.1
occ:1.00
|
NE2
|
A:HIS400
|
1.9
|
12.3
|
1.0
|
NE2
|
A:HIS65
|
2.0
|
13.9
|
1.0
|
O
|
A:HOH654
|
2.7
|
10.7
|
1.0
|
CE1
|
A:HIS400
|
2.8
|
13.0
|
1.0
|
CD2
|
A:HIS400
|
2.9
|
7.0
|
1.0
|
CE1
|
A:HIS65
|
2.9
|
15.4
|
1.0
|
CD2
|
A:HIS65
|
3.0
|
14.8
|
1.0
|
NE2
|
A:HIS402
|
3.4
|
13.2
|
1.0
|
ND1
|
A:HIS67
|
3.5
|
10.3
|
1.0
|
CD2
|
A:HIS402
|
3.5
|
13.7
|
1.0
|
CE1
|
A:HIS402
|
3.8
|
18.2
|
1.0
|
CG
|
A:HIS402
|
3.8
|
15.9
|
1.0
|
O
|
A:HOH944
|
3.8
|
15.0
|
0.5
|
N
|
A:GLY68
|
3.9
|
13.2
|
1.0
|
CA
|
A:HIS67
|
3.9
|
12.0
|
1.0
|
CE1
|
A:HIS67
|
3.9
|
9.0
|
1.0
|
CG
|
A:HIS67
|
3.9
|
11.5
|
1.0
|
ND1
|
A:HIS400
|
3.9
|
14.7
|
1.0
|
ND1
|
A:HIS402
|
4.0
|
14.7
|
1.0
|
CG
|
A:HIS400
|
4.0
|
10.9
|
1.0
|
ND1
|
A:HIS65
|
4.1
|
14.9
|
1.0
|
CU
|
A:CU502
|
4.1
|
15.8
|
1.0
|
CG
|
A:HIS65
|
4.1
|
14.7
|
1.0
|
CB
|
A:HIS67
|
4.3
|
11.8
|
1.0
|
CU
|
A:CU503
|
4.3
|
19.3
|
1.0
|
C
|
A:HIS67
|
4.4
|
12.6
|
1.0
|
NE2
|
A:HIS67
|
4.5
|
12.3
|
1.0
|
CD2
|
A:HIS67
|
4.5
|
10.7
|
1.0
|
CA
|
A:HIS402
|
4.5
|
16.7
|
1.0
|
O
|
A:HOH659
|
4.6
|
15.2
|
1.0
|
O
|
A:HOH621
|
4.7
|
14.7
|
1.0
|
CB
|
A:HIS402
|
4.7
|
16.4
|
1.0
|
N
|
A:HIS402
|
4.9
|
16.6
|
1.0
|
O
|
A:LEU401
|
4.9
|
17.3
|
1.0
|
CA
|
A:GLY68
|
5.0
|
12.7
|
1.0
|
N
|
A:HIS67
|
5.0
|
12.1
|
1.0
|
|
Copper binding site 5 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 5 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu501
b:20.7
occ:1.00
|
ND1
|
B:HIS397
|
1.9
|
21.3
|
1.0
|
ND1
|
B:HIS458
|
2.1
|
15.9
|
1.0
|
SG
|
B:CYS453
|
2.2
|
20.9
|
1.0
|
CE1
|
B:HIS397
|
2.8
|
25.3
|
1.0
|
CG
|
B:HIS397
|
3.1
|
20.4
|
1.0
|
CG
|
B:HIS458
|
3.1
|
17.6
|
1.0
|
CE1
|
B:HIS458
|
3.1
|
15.7
|
1.0
|
CB
|
B:CYS453
|
3.3
|
18.6
|
1.0
|
CB
|
B:HIS458
|
3.3
|
19.1
|
1.0
|
CB
|
B:HIS397
|
3.5
|
18.1
|
1.0
|
CD1
|
B:ILE455
|
3.8
|
19.4
|
1.0
|
CB
|
B:ILE455
|
3.8
|
19.6
|
1.0
|
CD2
|
B:PHE463
|
3.9
|
16.9
|
1.0
|
NE2
|
B:HIS397
|
4.0
|
24.2
|
1.0
|
CG1
|
B:ILE455
|
4.0
|
16.4
|
1.0
|
CA
|
B:HIS397
|
4.0
|
17.5
|
1.0
|
CD2
|
B:HIS397
|
4.1
|
26.7
|
1.0
|
CE2
|
B:PHE463
|
4.1
|
19.5
|
1.0
|
NE2
|
B:HIS458
|
4.2
|
13.7
|
1.0
|
CD2
|
B:HIS458
|
4.2
|
16.7
|
1.0
|
CG2
|
B:ILE455
|
4.6
|
13.3
|
1.0
|
CA
|
B:CYS453
|
4.7
|
19.7
|
1.0
|
N
|
B:ILE455
|
4.7
|
17.8
|
1.0
|
CD
|
B:PRO398
|
4.7
|
13.8
|
1.0
|
CA
|
B:ILE455
|
4.8
|
18.3
|
1.0
|
CA
|
B:HIS458
|
4.8
|
20.9
|
1.0
|
CZ
|
B:PHE341
|
4.8
|
24.5
|
1.0
|
CE1
|
B:PHE341
|
4.9
|
23.6
|
1.0
|
C
|
B:HIS397
|
5.0
|
17.9
|
1.0
|
|
Copper binding site 6 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 6 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu502
b:19.8
occ:1.00
|
NE2
|
B:HIS110
|
2.0
|
12.6
|
1.0
|
ND1
|
B:HIS67
|
2.0
|
15.9
|
1.0
|
NE2
|
B:HIS454
|
2.2
|
14.8
|
1.0
|
CD2
|
B:HIS110
|
2.9
|
14.6
|
1.0
|
CE1
|
B:HIS67
|
3.0
|
11.6
|
1.0
|
CG
|
B:HIS67
|
3.0
|
14.4
|
1.0
|
CE1
|
B:HIS454
|
3.0
|
16.9
|
1.0
|
CE1
|
B:HIS110
|
3.0
|
17.9
|
1.0
|
CD2
|
B:HIS454
|
3.2
|
16.3
|
1.0
|
CB
|
B:HIS67
|
3.3
|
13.5
|
1.0
|
CZ2
|
B:TRP108
|
3.8
|
8.3
|
1.0
|
CD2
|
B:HIS65
|
3.9
|
11.0
|
1.0
|
CU
|
B:CU504
|
4.0
|
26.5
|
1.0
|
CE2
|
B:TRP108
|
4.0
|
11.9
|
1.0
|
CG
|
B:HIS110
|
4.0
|
14.6
|
1.0
|
ND1
|
B:HIS110
|
4.1
|
13.2
|
1.0
|
NE2
|
B:HIS67
|
4.1
|
19.6
|
1.0
|
CD2
|
B:HIS67
|
4.1
|
14.3
|
1.0
|
NE1
|
B:TRP108
|
4.1
|
11.0
|
1.0
|
ND1
|
B:HIS454
|
4.2
|
13.4
|
1.0
|
CG
|
B:HIS454
|
4.3
|
15.2
|
1.0
|
CB
|
B:ALA244
|
4.3
|
14.5
|
1.0
|
CD2
|
B:HIS400
|
4.4
|
17.8
|
1.0
|
NE2
|
B:HIS65
|
4.5
|
19.9
|
1.0
|
NE2
|
B:HIS400
|
4.5
|
19.3
|
1.0
|
CH2
|
B:TRP108
|
4.5
|
12.9
|
1.0
|
CA
|
B:HIS67
|
4.5
|
16.7
|
1.0
|
O
|
B:HOH725
|
4.8
|
30.9
|
1.0
|
CD2
|
B:TRP108
|
5.0
|
9.7
|
1.0
|
|
Copper binding site 7 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 7 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu503
b:23.2
occ:1.00
|
NE2
|
B:HIS452
|
1.9
|
22.4
|
1.0
|
NE2
|
B:HIS112
|
2.1
|
19.3
|
1.0
|
NE2
|
B:HIS402
|
2.1
|
21.6
|
1.0
|
CD2
|
B:HIS452
|
2.9
|
25.2
|
1.0
|
CE1
|
B:HIS402
|
2.9
|
21.1
|
1.0
|
CE1
|
B:HIS452
|
3.0
|
22.2
|
1.0
|
CD2
|
B:HIS112
|
3.0
|
13.7
|
1.0
|
CE1
|
B:HIS112
|
3.1
|
18.5
|
1.0
|
CD2
|
B:HIS402
|
3.2
|
22.0
|
1.0
|
O
|
B:HOH725
|
3.6
|
30.9
|
1.0
|
CD2
|
B:PHE450
|
3.9
|
24.9
|
1.0
|
CG
|
B:HIS452
|
4.0
|
22.8
|
1.0
|
ND1
|
B:HIS452
|
4.0
|
22.8
|
1.0
|
ND1
|
B:HIS402
|
4.1
|
16.1
|
1.0
|
CD2
|
B:HIS400
|
4.1
|
17.8
|
1.0
|
CG
|
B:HIS112
|
4.1
|
17.9
|
1.0
|
ND1
|
B:HIS112
|
4.2
|
19.6
|
1.0
|
CG
|
B:HIS402
|
4.2
|
20.4
|
1.0
|
CU
|
B:CU504
|
4.3
|
26.5
|
1.0
|
CB
|
B:PHE450
|
4.4
|
25.7
|
1.0
|
CD2
|
B:HIS65
|
4.5
|
11.0
|
1.0
|
CG
|
B:PHE450
|
4.6
|
26.1
|
1.0
|
NE2
|
B:HIS65
|
4.7
|
19.9
|
1.0
|
NE2
|
B:HIS400
|
4.7
|
19.3
|
1.0
|
CE2
|
B:PHE450
|
4.8
|
24.7
|
1.0
|
NE2
|
B:HIS454
|
5.0
|
14.8
|
1.0
|
CE1
|
B:HIS110
|
5.0
|
17.9
|
1.0
|
|
Copper binding site 8 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 8 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu504
b:26.5
occ:1.00
|
NE2
|
B:HIS400
|
1.9
|
19.3
|
1.0
|
NE2
|
B:HIS65
|
2.0
|
19.9
|
1.0
|
O
|
B:HOH664
|
2.6
|
25.2
|
1.0
|
CD2
|
B:HIS65
|
2.9
|
11.0
|
1.0
|
CD2
|
B:HIS400
|
2.9
|
17.8
|
1.0
|
CE1
|
B:HIS400
|
3.0
|
17.2
|
1.0
|
CE1
|
B:HIS65
|
3.0
|
18.2
|
1.0
|
CD2
|
B:HIS402
|
3.3
|
22.0
|
1.0
|
NE2
|
B:HIS402
|
3.5
|
21.6
|
1.0
|
ND1
|
B:HIS67
|
3.5
|
15.9
|
1.0
|
CG
|
B:HIS67
|
3.7
|
14.4
|
1.0
|
CG
|
B:HIS402
|
3.8
|
20.4
|
1.0
|
CE1
|
B:HIS402
|
3.9
|
21.1
|
1.0
|
CA
|
B:HIS67
|
3.9
|
16.7
|
1.0
|
CE1
|
B:HIS67
|
3.9
|
11.6
|
1.0
|
CG
|
B:HIS65
|
4.0
|
16.3
|
1.0
|
CU
|
B:CU502
|
4.0
|
19.8
|
1.0
|
ND1
|
B:HIS400
|
4.0
|
20.6
|
1.0
|
ND1
|
B:HIS402
|
4.0
|
16.1
|
1.0
|
ND1
|
B:HIS65
|
4.1
|
16.6
|
1.0
|
CG
|
B:HIS400
|
4.1
|
17.5
|
1.0
|
N
|
B:GLY68
|
4.1
|
16.5
|
1.0
|
CB
|
B:HIS67
|
4.1
|
13.5
|
1.0
|
CD2
|
B:HIS67
|
4.3
|
14.3
|
1.0
|
CU
|
B:CU503
|
4.3
|
23.2
|
1.0
|
NE2
|
B:HIS67
|
4.4
|
19.6
|
1.0
|
CA
|
B:HIS402
|
4.5
|
22.2
|
1.0
|
C
|
B:HIS67
|
4.5
|
16.8
|
1.0
|
CB
|
B:HIS402
|
4.6
|
21.8
|
1.0
|
O
|
B:HOH695
|
4.7
|
23.3
|
1.0
|
O
|
B:HOH683
|
4.7
|
27.6
|
1.0
|
N
|
B:HIS402
|
4.9
|
21.4
|
1.0
|
O
|
B:LEU401
|
4.9
|
19.3
|
1.0
|
N
|
B:HIS67
|
5.0
|
17.8
|
1.0
|
|
Copper binding site 9 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 9 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu501
b:31.8
occ:1.00
|
ND1
|
C:HIS458
|
2.1
|
24.5
|
1.0
|
ND1
|
C:HIS397
|
2.2
|
36.4
|
1.0
|
SG
|
C:CYS453
|
2.2
|
26.9
|
1.0
|
CG
|
C:HIS458
|
3.1
|
22.9
|
1.0
|
CE1
|
C:HIS458
|
3.1
|
22.6
|
1.0
|
CG
|
C:HIS397
|
3.1
|
36.4
|
1.0
|
CE1
|
C:HIS397
|
3.2
|
36.6
|
1.0
|
CB
|
C:CYS453
|
3.4
|
26.0
|
1.0
|
CB
|
C:HIS458
|
3.4
|
27.4
|
1.0
|
CB
|
C:HIS397
|
3.4
|
32.7
|
1.0
|
CD1
|
C:ILE455
|
3.9
|
31.3
|
1.0
|
CD2
|
C:PHE463
|
3.9
|
31.0
|
1.0
|
CA
|
C:HIS397
|
3.9
|
32.5
|
1.0
|
CB
|
C:ILE455
|
3.9
|
25.6
|
1.0
|
CG1
|
C:ILE455
|
4.0
|
28.3
|
1.0
|
CE2
|
C:PHE463
|
4.0
|
28.1
|
1.0
|
NE2
|
C:HIS458
|
4.2
|
20.6
|
1.0
|
CD2
|
C:HIS458
|
4.2
|
23.9
|
1.0
|
NE2
|
C:HIS397
|
4.3
|
36.7
|
1.0
|
CD2
|
C:HIS397
|
4.3
|
37.9
|
1.0
|
CD
|
C:PRO398
|
4.6
|
28.2
|
1.0
|
CA
|
C:CYS453
|
4.7
|
25.8
|
1.0
|
O
|
C:GLY394
|
4.7
|
37.8
|
1.0
|
N
|
C:ILE455
|
4.7
|
24.6
|
1.0
|
N
|
C:HIS397
|
4.8
|
31.5
|
1.0
|
CG2
|
C:ILE455
|
4.9
|
27.0
|
1.0
|
CA
|
C:ILE455
|
4.9
|
25.5
|
1.0
|
CA
|
C:HIS458
|
4.9
|
27.6
|
1.0
|
CE1
|
C:PHE341
|
4.9
|
27.8
|
1.0
|
C
|
C:HIS397
|
5.0
|
31.1
|
1.0
|
O
|
C:ILE455
|
5.0
|
26.8
|
1.0
|
|
Copper binding site 10 out
of 12 in 3t6v
Go back to
Copper Binding Sites List in 3t6v
Copper binding site 10 out
of 12 in the Crystal Structure of Laccase From Steccherinum Ochraceum
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 Steccherinum Ochraceum within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu502
b:22.8
occ:1.00
|
ND1
|
C:HIS67
|
2.0
|
27.6
|
1.0
|
NE2
|
C:HIS110
|
2.1
|
21.9
|
1.0
|
NE2
|
C:HIS454
|
2.2
|
21.7
|
1.0
|
CE1
|
C:HIS67
|
2.9
|
21.6
|
1.0
|
CG
|
C:HIS67
|
3.0
|
21.0
|
1.0
|
CD2
|
C:HIS110
|
3.0
|
15.9
|
1.0
|
CE1
|
C:HIS454
|
3.0
|
21.0
|
1.0
|
CE1
|
C:HIS110
|
3.1
|
15.3
|
1.0
|
CD2
|
C:HIS454
|
3.4
|
26.7
|
1.0
|
CB
|
C:HIS67
|
3.4
|
22.5
|
1.0
|
CZ2
|
C:TRP108
|
3.8
|
16.8
|
1.0
|
CD2
|
C:HIS65
|
3.9
|
19.9
|
1.0
|
NE2
|
C:HIS67
|
4.0
|
21.4
|
1.0
|
CE2
|
C:TRP108
|
4.0
|
19.3
|
1.0
|
CD2
|
C:HIS67
|
4.1
|
19.8
|
1.0
|
CU
|
C:CU504
|
4.1
|
28.5
|
1.0
|
ND1
|
C:HIS110
|
4.1
|
19.2
|
1.0
|
CG
|
C:HIS110
|
4.2
|
18.7
|
1.0
|
NE1
|
C:TRP108
|
4.2
|
22.2
|
1.0
|
ND1
|
C:HIS454
|
4.2
|
26.7
|
1.0
|
CD2
|
C:HIS400
|
4.3
|
22.0
|
1.0
|
NE2
|
C:HIS400
|
4.3
|
16.9
|
1.0
|
CG
|
C:HIS454
|
4.4
|
23.4
|
1.0
|
CB
|
C:ALA244
|
4.4
|
18.9
|
1.0
|
CA
|
C:HIS67
|
4.5
|
22.6
|
1.0
|
CH2
|
C:TRP108
|
4.5
|
21.4
|
1.0
|
NE2
|
C:HIS65
|
4.5
|
23.3
|
1.0
|
O
|
C:HOH938
|
4.7
|
27.7
|
1.0
|
|
Reference:
M.Ferraroni,
I.Matera,
A.Chernykh,
M.Kolomytseva,
L.A.Golovleva,
A.Scozzafava,
F.Briganti.
Reaction Intermediates and Redox State Changes in A Blue Laccase From Steccherinum Ochraceum Observed By Crystallographic High/Low X-Ray Dose Experiments. J.Inorg.Biochem. V. 111 203 2012.
ISSN: ISSN 0162-0134
PubMed: 22341982
DOI: 10.1016/J.JINORGBIO.2012.01.011
Page generated: Wed Jul 31 01:46:40 2024
|