Copper in PDB 7puh: Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
Enzymatic activity of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
All present enzymatic activity of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus:
1.10.3.2;
Protein crystallography data
The structure of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus, PDB code: 7puh
was solved by
I.Kolyadenko,
S.Tishchenko,
A.Gabdulkhakov,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.41 /
1.30
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
74.76,
94.286,
120.482,
90,
91.27,
90
|
R / Rfree (%)
|
13.3 /
15.7
|
Copper Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
24;
Binding sites:
The binding sites of Copper atom in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
(pdb code 7puh). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 24 binding sites of Copper where determined in the
Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus, PDB code: 7puh:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Copper binding site 1 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 1 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_01.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_01_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu401
b:14.8
occ:0.95
|
ND1
|
A:HIS232
|
2.0
|
12.8
|
1.0
|
ND1
|
A:HIS294
|
2.0
|
13.5
|
1.0
|
SG
|
A:CYS289
|
2.2
|
14.0
|
1.0
|
CE1
|
A:HIS232
|
2.9
|
13.5
|
1.0
|
CG
|
A:HIS232
|
3.0
|
13.1
|
1.0
|
CE1
|
A:HIS294
|
3.0
|
14.3
|
1.0
|
CG
|
A:HIS294
|
3.0
|
13.6
|
1.0
|
CB
|
A:CYS289
|
3.2
|
13.6
|
1.0
|
CB
|
A:HIS294
|
3.3
|
13.1
|
1.0
|
CB
|
A:HIS232
|
3.4
|
13.4
|
1.0
|
SD
|
A:MET299
|
3.6
|
22.9
|
1.0
|
CA
|
A:HIS232
|
3.7
|
12.5
|
1.0
|
CE
|
A:MET299
|
3.9
|
22.9
|
1.0
|
NE2
|
A:HIS232
|
4.1
|
13.8
|
1.0
|
NE2
|
A:HIS294
|
4.1
|
14.9
|
1.0
|
CD2
|
A:HIS232
|
4.1
|
13.8
|
1.0
|
CD2
|
A:HIS294
|
4.1
|
14.2
|
1.0
|
CB
|
A:VAL291
|
4.1
|
12.8
|
1.0
|
CG2
|
A:VAL291
|
4.1
|
13.1
|
1.0
|
O
|
A:TYR231
|
4.1
|
12.7
|
1.0
|
CA
|
A:CYS289
|
4.6
|
12.8
|
1.0
|
N
|
A:THR233
|
4.6
|
13.1
|
1.0
|
N
|
A:HIS232
|
4.8
|
12.8
|
1.0
|
C
|
A:HIS232
|
4.8
|
13.2
|
1.0
|
CD2
|
A:PHE196
|
4.8
|
16.6
|
1.0
|
CA
|
A:HIS294
|
4.8
|
13.5
|
1.0
|
C
|
A:TYR231
|
4.9
|
12.4
|
1.0
|
CG1
|
A:VAL291
|
5.0
|
14.3
|
1.0
|
CE2
|
A:PHE196
|
5.0
|
16.9
|
1.0
|
|
Copper binding site 2 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 2 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_02.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_02_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu402
b:24.9
occ:0.84
|
NE2
|
A:HIS237
|
2.0
|
17.9
|
1.0
|
NE2
|
A:HIS288
|
2.1
|
19.4
|
1.0
|
O2
|
A:OXY404
|
2.1
|
25.8
|
0.7
|
NE2
|
C:HIS159
|
2.1
|
20.2
|
1.0
|
O1
|
A:OXY404
|
2.4
|
23.7
|
0.7
|
CE1
|
A:HIS237
|
2.9
|
18.0
|
1.0
|
CE1
|
A:HIS288
|
3.0
|
19.8
|
1.0
|
CE1
|
C:HIS159
|
3.1
|
20.1
|
1.0
|
CD2
|
C:HIS159
|
3.1
|
19.1
|
1.0
|
CD2
|
A:HIS288
|
3.1
|
19.7
|
1.0
|
CD2
|
A:HIS237
|
3.1
|
17.6
|
1.0
|
O
|
C:HOH580
|
3.8
|
32.6
|
1.0
|
CD2
|
A:HIS235
|
3.9
|
16.4
|
1.0
|
O
|
A:HOH510
|
3.9
|
50.1
|
1.0
|
CU
|
C:CU402
|
4.0
|
17.7
|
0.3
|
CE
|
A:MET286
|
4.0
|
37.1
|
1.0
|
ND1
|
A:HIS237
|
4.1
|
17.7
|
1.0
|
ND1
|
A:HIS288
|
4.1
|
18.7
|
1.0
|
CG
|
A:HIS237
|
4.2
|
16.6
|
1.0
|
CG
|
A:HIS288
|
4.2
|
17.1
|
1.0
|
ND1
|
C:HIS159
|
4.2
|
18.8
|
1.0
|
CG
|
C:HIS159
|
4.3
|
18.0
|
1.0
|
NE2
|
A:HIS235
|
4.3
|
17.1
|
1.0
|
NE2
|
C:HIS103
|
4.3
|
22.8
|
1.0
|
CU
|
C:CU401
|
4.5
|
21.6
|
0.6
|
CD2
|
C:HIS103
|
4.5
|
22.0
|
1.0
|
NE2
|
A:HIS290
|
4.6
|
16.2
|
1.0
|
CD2
|
A:HIS290
|
4.8
|
15.1
|
1.0
|
CE1
|
C:HIS103
|
4.9
|
21.9
|
1.0
|
SD
|
A:MET286
|
4.9
|
37.3
|
1.0
|
|
Copper binding site 3 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 3 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_03.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_03_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu403
b:17.5
occ:0.46
|
NE2
|
A:HIS157
|
2.1
|
16.5
|
1.0
|
NE2
|
B:HIS290
|
2.1
|
16.0
|
1.0
|
O2
|
B:OXY406
|
2.1
|
19.2
|
0.7
|
NE2
|
A:HIS105
|
2.2
|
14.4
|
1.0
|
O1
|
B:OXY406
|
2.4
|
24.1
|
0.7
|
CE1
|
A:HIS157
|
2.7
|
16.8
|
1.0
|
CE1
|
A:HIS105
|
3.0
|
13.8
|
1.0
|
CD2
|
B:HIS290
|
3.0
|
14.1
|
1.0
|
CE1
|
B:HIS290
|
3.1
|
15.9
|
1.0
|
CD2
|
A:HIS157
|
3.3
|
15.2
|
1.0
|
CD2
|
A:HIS105
|
3.3
|
14.6
|
1.0
|
CU
|
B:CU403
|
3.6
|
18.0
|
0.3
|
CD2
|
A:HIS103
|
3.7
|
17.0
|
1.0
|
NE2
|
B:HIS235
|
4.0
|
16.1
|
1.0
|
ND1
|
A:HIS157
|
4.0
|
15.7
|
1.0
|
CD2
|
B:HIS235
|
4.1
|
15.2
|
1.0
|
ND1
|
A:HIS105
|
4.1
|
13.0
|
1.0
|
NE2
|
A:HIS103
|
4.2
|
17.8
|
1.0
|
ND1
|
B:HIS290
|
4.2
|
14.4
|
1.0
|
CG
|
B:HIS290
|
4.2
|
13.1
|
1.0
|
CB
|
A:ALA267
|
4.2
|
14.3
|
1.0
|
CG
|
A:HIS157
|
4.3
|
14.3
|
1.0
|
CG
|
A:HIS105
|
4.3
|
12.8
|
1.0
|
CU
|
B:CU402
|
4.4
|
19.9
|
0.9
|
O
|
A:HOH600
|
4.5
|
30.9
|
1.0
|
CE1
|
A:HIS155
|
4.6
|
14.9
|
1.0
|
CE1
|
B:HIS235
|
4.6
|
15.6
|
1.0
|
CG
|
B:HIS235
|
4.8
|
14.8
|
1.0
|
CG
|
A:HIS103
|
5.0
|
16.5
|
1.0
|
|
Copper binding site 4 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 4 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_04.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_04_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu401
b:13.4
occ:1.00
|
ND1
|
B:HIS294
|
2.0
|
12.6
|
1.0
|
ND1
|
B:HIS232
|
2.0
|
11.1
|
1.0
|
SG
|
B:CYS289
|
2.2
|
12.5
|
1.0
|
CE1
|
B:HIS232
|
3.0
|
12.4
|
1.0
|
CE1
|
B:HIS294
|
3.0
|
13.9
|
1.0
|
CG
|
B:HIS294
|
3.0
|
11.8
|
1.0
|
CG
|
B:HIS232
|
3.0
|
11.6
|
1.0
|
CB
|
B:CYS289
|
3.2
|
11.6
|
1.0
|
CB
|
B:HIS294
|
3.3
|
11.5
|
1.0
|
CB
|
B:HIS232
|
3.4
|
12.2
|
1.0
|
SD
|
B:MET299
|
3.5
|
17.2
|
1.0
|
CA
|
B:HIS232
|
3.8
|
11.8
|
1.0
|
CE
|
B:MET299
|
4.0
|
17.8
|
1.0
|
NE2
|
B:HIS294
|
4.1
|
14.0
|
1.0
|
NE2
|
B:HIS232
|
4.1
|
12.3
|
1.0
|
CG2
|
B:VAL291
|
4.1
|
12.4
|
1.0
|
CD2
|
B:HIS294
|
4.1
|
13.8
|
1.0
|
CD2
|
B:HIS232
|
4.1
|
12.4
|
1.0
|
CB
|
B:VAL291
|
4.1
|
11.9
|
1.0
|
O
|
B:TYR231
|
4.2
|
12.0
|
1.0
|
CA
|
B:CYS289
|
4.6
|
11.1
|
1.0
|
N
|
B:THR233
|
4.6
|
11.3
|
1.0
|
N
|
B:HIS232
|
4.8
|
11.5
|
1.0
|
C
|
B:HIS232
|
4.8
|
11.3
|
1.0
|
CA
|
B:HIS294
|
4.8
|
12.1
|
1.0
|
C
|
B:TYR231
|
4.9
|
10.8
|
1.0
|
CD2
|
B:PHE196
|
4.9
|
15.9
|
1.0
|
CG
|
B:MET299
|
4.9
|
16.4
|
1.0
|
|
Copper binding site 5 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 5 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_05.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_05_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu402
b:19.9
occ:0.88
|
NE2
|
B:HIS237
|
2.0
|
15.9
|
1.0
|
NE2
|
B:HIS288
|
2.1
|
16.7
|
1.0
|
NE2
|
A:HIS159
|
2.1
|
16.8
|
1.0
|
O1
|
B:OXY406
|
2.1
|
24.1
|
0.7
|
O2
|
B:OXY406
|
2.4
|
19.2
|
0.7
|
CE1
|
B:HIS237
|
2.9
|
16.3
|
1.0
|
CE1
|
B:HIS288
|
2.9
|
16.8
|
1.0
|
CE1
|
A:HIS159
|
3.1
|
16.5
|
1.0
|
CD2
|
B:HIS288
|
3.1
|
16.8
|
1.0
|
CD2
|
A:HIS159
|
3.1
|
15.9
|
1.0
|
CD2
|
B:HIS237
|
3.2
|
16.4
|
1.0
|
O
|
A:HOH600
|
3.7
|
30.9
|
1.0
|
CD2
|
B:HIS235
|
3.9
|
15.2
|
1.0
|
O
|
B:HOH510
|
3.9
|
39.2
|
1.0
|
SD
|
B:MET286
|
4.0
|
25.3
|
0.6
|
CU
|
B:CU403
|
4.0
|
18.0
|
0.3
|
ND1
|
B:HIS237
|
4.1
|
15.9
|
1.0
|
ND1
|
B:HIS288
|
4.1
|
17.3
|
1.0
|
ND1
|
A:HIS159
|
4.2
|
16.4
|
1.0
|
CG
|
B:HIS288
|
4.2
|
15.1
|
1.0
|
CG
|
B:HIS237
|
4.2
|
14.6
|
1.0
|
CG
|
A:HIS159
|
4.3
|
15.2
|
1.0
|
NE2
|
B:HIS235
|
4.3
|
16.1
|
1.0
|
CG
|
B:MET286
|
4.4
|
22.6
|
0.6
|
CU
|
A:CU403
|
4.4
|
17.5
|
0.5
|
NE2
|
A:HIS103
|
4.4
|
17.8
|
1.0
|
CE
|
B:MET286
|
4.5
|
27.2
|
0.5
|
NE2
|
B:HIS290
|
4.5
|
16.0
|
1.0
|
CD2
|
A:HIS103
|
4.6
|
17.0
|
1.0
|
CD2
|
B:HIS290
|
4.8
|
14.1
|
1.0
|
CE1
|
A:HIS103
|
5.0
|
17.1
|
1.0
|
|
Copper binding site 6 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 6 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_06.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_06_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu403
b:18.0
occ:0.26
|
NE2
|
A:HIS103
|
1.8
|
17.8
|
1.0
|
NE2
|
B:HIS235
|
1.8
|
16.1
|
1.0
|
O2
|
B:OXY406
|
2.5
|
19.2
|
0.7
|
CD2
|
A:HIS103
|
2.7
|
17.0
|
1.0
|
CE1
|
B:HIS235
|
2.7
|
15.6
|
1.0
|
CE1
|
A:HIS103
|
2.8
|
17.1
|
1.0
|
O
|
A:HOH503
|
2.9
|
29.1
|
1.0
|
CD2
|
B:HIS235
|
2.9
|
15.2
|
1.0
|
CD2
|
B:HIS237
|
3.4
|
16.4
|
1.0
|
NE2
|
B:HIS237
|
3.4
|
15.9
|
1.0
|
CU
|
A:CU403
|
3.6
|
17.5
|
0.5
|
NE2
|
A:HIS105
|
3.7
|
14.4
|
1.0
|
O1
|
B:OXY406
|
3.7
|
24.1
|
0.7
|
ND1
|
A:HIS103
|
3.8
|
18.0
|
1.0
|
CG
|
B:HIS237
|
3.8
|
14.6
|
1.0
|
CG
|
A:HIS103
|
3.9
|
16.5
|
1.0
|
ND1
|
B:HIS235
|
3.9
|
14.7
|
1.0
|
CE1
|
B:HIS237
|
3.9
|
16.3
|
1.0
|
CE1
|
A:HIS105
|
3.9
|
13.8
|
1.0
|
CD2
|
A:HIS105
|
4.0
|
14.6
|
1.0
|
CG
|
B:HIS235
|
4.0
|
14.8
|
1.0
|
CU
|
B:CU402
|
4.0
|
19.9
|
0.9
|
ND1
|
B:HIS237
|
4.1
|
15.9
|
1.0
|
O
|
A:VAL104
|
4.3
|
15.9
|
1.0
|
ND1
|
A:HIS105
|
4.3
|
13.0
|
1.0
|
CG
|
A:HIS105
|
4.4
|
12.8
|
1.0
|
OH
|
A:TYR109
|
4.4
|
27.9
|
1.0
|
CA
|
B:HIS237
|
4.5
|
13.9
|
1.0
|
CB
|
B:HIS237
|
4.7
|
15.1
|
1.0
|
O
|
B:HOH535
|
4.8
|
22.9
|
1.0
|
N
|
B:HIS237
|
4.8
|
13.7
|
1.0
|
O
|
B:MET236
|
4.9
|
16.6
|
1.0
|
OD2
|
B:ASP260
|
4.9
|
15.0
|
1.0
|
NE2
|
A:HIS157
|
4.9
|
16.5
|
1.0
|
C
|
A:VAL104
|
4.9
|
14.3
|
1.0
|
|
Copper binding site 7 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 7 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_07.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_07_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu404
b:21.9
occ:0.31
|
NE2
|
B:HIS157
|
2.1
|
14.9
|
1.0
|
O1
|
C:OXY405
|
2.1
|
12.9
|
0.6
|
NE2
|
C:HIS290
|
2.2
|
16.1
|
1.0
|
NE2
|
B:HIS105
|
2.2
|
15.0
|
1.0
|
O2
|
C:OXY405
|
2.4
|
18.5
|
0.6
|
CE1
|
B:HIS157
|
2.6
|
14.6
|
1.0
|
CE1
|
B:HIS105
|
2.9
|
14.7
|
1.0
|
CD2
|
C:HIS290
|
3.1
|
14.2
|
1.0
|
CE1
|
C:HIS290
|
3.2
|
16.0
|
1.0
|
CD2
|
B:HIS157
|
3.4
|
14.1
|
1.0
|
CD2
|
B:HIS105
|
3.4
|
15.0
|
1.0
|
CU
|
B:CU405
|
3.6
|
55.5
|
0.2
|
CD2
|
B:HIS103
|
3.6
|
16.6
|
1.0
|
NE2
|
C:HIS235
|
3.9
|
16.9
|
1.0
|
ND1
|
B:HIS157
|
3.9
|
13.5
|
1.0
|
CD2
|
C:HIS235
|
4.0
|
16.4
|
1.0
|
NE2
|
B:HIS103
|
4.1
|
17.4
|
1.0
|
ND1
|
B:HIS105
|
4.1
|
13.2
|
1.0
|
CB
|
B:ALA267
|
4.2
|
14.4
|
1.0
|
CG
|
C:HIS290
|
4.2
|
13.4
|
1.0
|
ND1
|
C:HIS290
|
4.2
|
14.4
|
1.0
|
CG
|
B:HIS157
|
4.3
|
12.8
|
1.0
|
CG
|
B:HIS105
|
4.4
|
13.4
|
1.0
|
CU
|
C:CU404
|
4.4
|
18.1
|
1.0
|
O
|
B:HOH580
|
4.5
|
27.4
|
1.0
|
CE1
|
C:HIS235
|
4.6
|
17.8
|
1.0
|
CE1
|
B:HIS155
|
4.7
|
13.6
|
1.0
|
CG
|
C:HIS235
|
4.8
|
16.2
|
1.0
|
CG
|
B:HIS103
|
4.9
|
14.4
|
1.0
|
CD2
|
B:HIS159
|
4.9
|
14.0
|
1.0
|
|
Copper binding site 8 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 8 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_08.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_08_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu405
b:55.5
occ:0.22
|
NE2
|
B:HIS103
|
1.7
|
17.4
|
1.0
|
NE2
|
C:HIS235
|
1.7
|
16.9
|
1.0
|
CE1
|
C:HIS235
|
2.6
|
17.8
|
1.0
|
CE1
|
B:HIS103
|
2.7
|
17.1
|
1.0
|
O1
|
C:OXY405
|
2.7
|
12.9
|
0.6
|
CD2
|
B:HIS103
|
2.7
|
16.6
|
1.0
|
CD2
|
C:HIS235
|
2.8
|
16.4
|
1.0
|
O
|
B:HOH501
|
2.9
|
30.8
|
1.0
|
CD2
|
C:HIS237
|
3.2
|
14.5
|
1.0
|
NE2
|
C:HIS237
|
3.3
|
14.5
|
1.0
|
CU
|
B:CU404
|
3.6
|
21.9
|
0.3
|
CG
|
C:HIS237
|
3.8
|
15.0
|
1.0
|
ND1
|
B:HIS103
|
3.8
|
16.1
|
1.0
|
CE1
|
C:HIS237
|
3.8
|
15.9
|
1.0
|
ND1
|
C:HIS235
|
3.8
|
16.8
|
1.0
|
NE2
|
B:HIS105
|
3.8
|
15.0
|
1.0
|
CG
|
B:HIS103
|
3.8
|
14.4
|
1.0
|
O2
|
C:OXY405
|
3.9
|
18.5
|
0.6
|
CG
|
C:HIS235
|
3.9
|
16.2
|
1.0
|
CU
|
C:CU404
|
3.9
|
18.1
|
1.0
|
CE1
|
B:HIS105
|
4.0
|
14.7
|
1.0
|
ND1
|
C:HIS237
|
4.1
|
15.0
|
1.0
|
CD2
|
B:HIS105
|
4.2
|
15.0
|
1.0
|
OH
|
B:TYR109
|
4.3
|
26.0
|
1.0
|
ND1
|
B:HIS105
|
4.4
|
13.2
|
1.0
|
CA
|
C:HIS237
|
4.4
|
14.3
|
1.0
|
O
|
B:VAL104
|
4.5
|
14.7
|
1.0
|
CG
|
B:HIS105
|
4.5
|
13.4
|
1.0
|
O
|
C:MET236
|
4.6
|
18.4
|
0.6
|
CB
|
C:HIS237
|
4.6
|
14.7
|
1.0
|
N
|
C:HIS237
|
4.8
|
14.6
|
1.0
|
OD2
|
C:ASP260
|
4.9
|
14.9
|
1.0
|
C
|
C:MET236
|
4.9
|
16.2
|
0.6
|
O
|
C:HOH536
|
4.9
|
24.5
|
1.0
|
|
Copper binding site 9 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 9 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_09.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_09_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 9 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu401
b:21.6
occ:0.56
|
NE2
|
C:HIS157
|
2.0
|
18.6
|
1.0
|
NE2
|
A:HIS290
|
2.1
|
16.2
|
1.0
|
NE2
|
C:HIS105
|
2.1
|
15.9
|
1.0
|
O1
|
A:OXY404
|
2.3
|
23.7
|
0.7
|
O2
|
A:OXY404
|
2.5
|
25.8
|
0.7
|
CE1
|
C:HIS157
|
2.7
|
18.3
|
1.0
|
CE1
|
C:HIS105
|
3.0
|
15.3
|
1.0
|
CD2
|
A:HIS290
|
3.0
|
15.1
|
1.0
|
CE1
|
A:HIS290
|
3.1
|
16.4
|
1.0
|
CD2
|
C:HIS105
|
3.2
|
16.1
|
1.0
|
CD2
|
C:HIS157
|
3.2
|
17.1
|
1.0
|
CU
|
C:CU402
|
3.7
|
17.7
|
0.3
|
CD2
|
C:HIS103
|
3.8
|
22.0
|
1.0
|
ND1
|
C:HIS157
|
3.9
|
17.6
|
1.0
|
NE2
|
A:HIS235
|
4.1
|
17.1
|
1.0
|
ND1
|
A:HIS290
|
4.1
|
15.5
|
1.0
|
ND1
|
C:HIS105
|
4.2
|
14.7
|
1.0
|
CB
|
C:ALA267
|
4.2
|
15.8
|
1.0
|
CD2
|
A:HIS235
|
4.2
|
16.4
|
1.0
|
CG
|
A:HIS290
|
4.2
|
14.8
|
1.0
|
CG
|
C:HIS157
|
4.2
|
16.2
|
1.0
|
NE2
|
C:HIS103
|
4.2
|
22.8
|
1.0
|
CG
|
C:HIS105
|
4.3
|
15.0
|
1.0
|
O
|
C:HOH580
|
4.4
|
32.6
|
1.0
|
CU
|
A:CU402
|
4.5
|
24.9
|
0.8
|
CE1
|
C:HIS155
|
4.5
|
15.7
|
1.0
|
CE1
|
A:HIS235
|
4.7
|
16.5
|
1.0
|
CG
|
A:HIS235
|
4.9
|
16.0
|
1.0
|
CG
|
C:HIS103
|
5.0
|
20.2
|
1.0
|
|
Copper binding site 10 out
of 24 in 7puh
Go back to
Copper Binding Sites List in 7puh
Copper binding site 10 out
of 24 in the Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus
![](/pictures/CU/pdb/pu/7puh-CU-sphere_10.jpg) Mono view
![](/pictures/CU/pdb/pu/7puh-CU-sphere_10_stereo.jpg) Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 10 of Crystal Structure of Two-Domain Laccase Mutant H165A/R240H From Streptomyces Griseoflavus within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu402
b:17.7
occ:0.27
|
NE2
|
C:HIS103
|
1.7
|
22.8
|
1.0
|
NE2
|
A:HIS235
|
1.8
|
17.1
|
1.0
|
O1
|
A:OXY404
|
2.4
|
23.7
|
0.7
|
CD2
|
C:HIS103
|
2.7
|
22.0
|
1.0
|
CE1
|
A:HIS235
|
2.7
|
16.5
|
1.0
|
CE1
|
C:HIS103
|
2.8
|
21.9
|
1.0
|
CD2
|
A:HIS235
|
2.9
|
16.4
|
1.0
|
O
|
C:HOH505
|
3.0
|
28.9
|
1.0
|
CD2
|
A:HIS237
|
3.3
|
17.6
|
1.0
|
NE2
|
A:HIS237
|
3.4
|
17.9
|
1.0
|
O2
|
A:OXY404
|
3.6
|
25.8
|
0.7
|
NE2
|
C:HIS105
|
3.6
|
15.9
|
1.0
|
CU
|
C:CU401
|
3.7
|
21.6
|
0.6
|
CG
|
A:HIS237
|
3.8
|
16.6
|
1.0
|
ND1
|
C:HIS103
|
3.8
|
21.9
|
1.0
|
CG
|
C:HIS103
|
3.9
|
20.2
|
1.0
|
ND1
|
A:HIS235
|
3.9
|
15.9
|
1.0
|
CE1
|
C:HIS105
|
3.9
|
15.3
|
1.0
|
CD2
|
C:HIS105
|
4.0
|
16.1
|
1.0
|
CU
|
A:CU402
|
4.0
|
24.9
|
0.8
|
CE1
|
A:HIS237
|
4.0
|
18.0
|
1.0
|
CG
|
A:HIS235
|
4.0
|
16.0
|
1.0
|
ND1
|
A:HIS237
|
4.2
|
17.7
|
1.0
|
O
|
C:VAL104
|
4.3
|
16.9
|
1.0
|
ND1
|
C:HIS105
|
4.4
|
14.7
|
1.0
|
CG
|
C:HIS105
|
4.4
|
15.0
|
1.0
|
CA
|
A:HIS237
|
4.4
|
15.3
|
1.0
|
OH
|
C:TYR109
|
4.5
|
28.7
|
1.0
|
CB
|
A:HIS237
|
4.7
|
15.8
|
1.0
|
N
|
A:HIS237
|
4.8
|
15.4
|
1.0
|
OD2
|
A:ASP260
|
4.9
|
16.1
|
1.0
|
O
|
A:MET236
|
5.0
|
18.1
|
1.0
|
C
|
C:VAL104
|
5.0
|
16.4
|
1.0
|
O
|
A:HOH541
|
5.0
|
23.8
|
1.0
|
|
Reference:
I.Kolyadenko,
A.Scherbakova,
K.Kovalev,
A.Gabdulkhakov,
S.Tishchenko.
Engineering the Catalytic Properties of Two-Domain Laccase From Streptomyces Griseoflavus Ac-993. Int J Mol Sci V. 23 2021.
ISSN: ESSN 1422-0067
PubMed: 35008493
DOI: 10.3390/IJMS23010065
Page generated: Wed Jul 31 08:44:48 2024
|