Copper in PDB 5mhy: The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
Enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
All present enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.:
1.10.3.2;
Protein crystallography data
The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min., PDB code: 5mhy
was solved by
K.M.Polyakov,
S.Gavryushov,
T.V.Fedorova,
O.A.Glazunova,
A.N.Popov,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
67.53 /
1.35
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.380,
84.420,
112.520,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
13.2 /
14.5
|
Other elements in 5mhy:
The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min. also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
(pdb code 5mhy). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min., PDB code: 5mhy:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 5mhy
Go back to
Copper Binding Sites List in 5mhy
Copper binding site 1 out
of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:7.4
occ:0.45
|
CU
|
A:CU601
|
0.0
|
7.4
|
0.5
|
CU
|
A:CU601
|
0.7
|
5.5
|
0.5
|
O
|
A:HOH704
|
1.6
|
3.6
|
0.2
|
O2
|
A:OXY609
|
1.9
|
9.4
|
0.4
|
O1
|
A:OXY609
|
1.9
|
6.8
|
0.4
|
O
|
A:HOH701
|
2.0
|
9.0
|
0.4
|
NE2
|
A:HIS402
|
2.1
|
6.1
|
1.0
|
NE2
|
A:HIS452
|
2.1
|
9.1
|
1.0
|
NE2
|
A:HIS112
|
2.2
|
7.1
|
1.0
|
O
|
A:HOH705
|
2.5
|
10.3
|
0.4
|
CE1
|
A:HIS402
|
2.9
|
6.2
|
1.0
|
CE1
|
A:HIS452
|
3.0
|
9.0
|
1.0
|
HD2
|
A:HIS400
|
3.0
|
6.2
|
1.0
|
CD2
|
A:HIS112
|
3.0
|
6.7
|
1.0
|
HE1
|
A:HIS402
|
3.1
|
6.1
|
1.0
|
HE1
|
A:HIS452
|
3.1
|
8.8
|
1.0
|
HD2
|
A:HIS112
|
3.1
|
6.8
|
1.0
|
CD2
|
A:HIS402
|
3.1
|
5.9
|
1.0
|
CE1
|
A:HIS112
|
3.3
|
7.5
|
1.0
|
CD2
|
A:HIS452
|
3.3
|
7.6
|
1.0
|
HD2
|
A:HIS402
|
3.4
|
6.0
|
1.0
|
HE1
|
A:HIS112
|
3.5
|
7.3
|
1.0
|
HD2
|
A:HIS452
|
3.5
|
7.8
|
1.0
|
O
|
A:HOH702
|
3.6
|
13.5
|
0.5
|
CD2
|
A:HIS400
|
3.8
|
6.2
|
1.0
|
HE1
|
A:HIS110
|
3.9
|
6.7
|
1.0
|
HD2
|
A:PHE450
|
3.9
|
7.7
|
1.0
|
CU
|
A:CU603
|
3.9
|
6.5
|
0.8
|
HD2
|
A:HIS65
|
3.9
|
6.2
|
1.0
|
CD2
|
A:HIS65
|
4.1
|
6.1
|
1.0
|
O1
|
A:OXY610
|
4.1
|
12.3
|
0.5
|
ND1
|
A:HIS402
|
4.1
|
5.9
|
1.0
|
CU
|
A:CU602
|
4.1
|
11.4
|
0.5
|
HB3
|
A:PHE450
|
4.2
|
6.7
|
1.0
|
NE2
|
A:HIS65
|
4.2
|
6.4
|
1.0
|
ND1
|
A:HIS452
|
4.2
|
8.0
|
1.0
|
CG
|
A:HIS402
|
4.2
|
5.9
|
1.0
|
CG
|
A:HIS112
|
4.3
|
6.8
|
1.0
|
NE2
|
A:HIS400
|
4.3
|
6.1
|
1.0
|
ND1
|
A:HIS112
|
4.3
|
7.0
|
1.0
|
CG
|
A:HIS452
|
4.4
|
7.0
|
1.0
|
HB3
|
A:PRO80
|
4.4
|
6.2
|
1.0
|
CD2
|
A:PHE450
|
4.6
|
7.9
|
1.0
|
HD2
|
A:HIS454
|
4.6
|
6.6
|
1.0
|
CE1
|
A:HIS110
|
4.7
|
6.9
|
1.0
|
O2
|
A:OXY610
|
4.7
|
13.7
|
0.5
|
NE2
|
A:HIS454
|
4.7
|
6.9
|
1.0
|
CU
|
A:CU602
|
4.7
|
4.5
|
0.5
|
HD21
|
A:LEU459
|
4.7
|
8.7
|
1.0
|
CD2
|
A:HIS454
|
4.8
|
6.7
|
1.0
|
CG
|
A:HIS65
|
4.8
|
6.2
|
1.0
|
HD1
|
A:HIS402
|
4.9
|
6.0
|
1.0
|
CE1
|
A:HIS65
|
4.9
|
6.3
|
1.0
|
HD1
|
A:HIS452
|
4.9
|
8.0
|
1.0
|
CB
|
A:PHE450
|
5.0
|
6.7
|
1.0
|
|
Copper binding site 2 out
of 6 in 5mhy
Go back to
Copper Binding Sites List in 5mhy
Copper binding site 2 out
of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:5.5
occ:0.45
|
CU
|
A:CU601
|
0.0
|
5.5
|
0.5
|
CU
|
A:CU601
|
0.7
|
7.4
|
0.5
|
NE2
|
A:HIS452
|
1.9
|
9.1
|
1.0
|
NE2
|
A:HIS402
|
2.0
|
6.1
|
1.0
|
NE2
|
A:HIS112
|
2.0
|
7.1
|
1.0
|
O
|
A:HOH704
|
2.4
|
3.6
|
0.2
|
O2
|
A:OXY609
|
2.5
|
9.4
|
0.4
|
O1
|
A:OXY609
|
2.6
|
6.8
|
0.4
|
O
|
A:HOH701
|
2.7
|
9.0
|
0.4
|
CD2
|
A:HIS452
|
2.8
|
7.6
|
1.0
|
CE1
|
A:HIS402
|
2.8
|
6.2
|
1.0
|
CE1
|
A:HIS112
|
2.9
|
7.5
|
1.0
|
HE1
|
A:HIS402
|
3.0
|
6.1
|
1.0
|
HD2
|
A:HIS452
|
3.0
|
7.8
|
1.0
|
CE1
|
A:HIS452
|
3.0
|
9.0
|
1.0
|
HE1
|
A:HIS112
|
3.0
|
7.3
|
1.0
|
CD2
|
A:HIS402
|
3.1
|
5.9
|
1.0
|
CD2
|
A:HIS112
|
3.1
|
6.7
|
1.0
|
HD2
|
A:PHE450
|
3.2
|
7.7
|
1.0
|
O
|
A:HOH705
|
3.2
|
10.3
|
0.4
|
HE1
|
A:HIS452
|
3.3
|
8.8
|
1.0
|
HD2
|
A:HIS402
|
3.4
|
6.0
|
1.0
|
HD2
|
A:HIS112
|
3.4
|
6.8
|
1.0
|
HD2
|
A:HIS400
|
3.4
|
6.2
|
1.0
|
HB3
|
A:PHE450
|
3.6
|
6.7
|
1.0
|
O
|
A:HOH702
|
3.8
|
13.5
|
0.5
|
CD2
|
A:PHE450
|
3.9
|
7.9
|
1.0
|
CG
|
A:HIS452
|
4.0
|
7.0
|
1.0
|
ND1
|
A:HIS402
|
4.0
|
5.9
|
1.0
|
HB3
|
A:PRO80
|
4.0
|
6.2
|
1.0
|
ND1
|
A:HIS452
|
4.0
|
8.0
|
1.0
|
ND1
|
A:HIS112
|
4.1
|
7.0
|
1.0
|
CG
|
A:HIS402
|
4.1
|
5.9
|
1.0
|
CG
|
A:HIS112
|
4.2
|
6.8
|
1.0
|
CD2
|
A:HIS400
|
4.3
|
6.2
|
1.0
|
O1
|
A:OXY610
|
4.3
|
12.3
|
0.5
|
HE1
|
A:HIS110
|
4.4
|
6.7
|
1.0
|
CB
|
A:PHE450
|
4.4
|
6.7
|
1.0
|
HD21
|
A:LEU459
|
4.4
|
8.7
|
1.0
|
CU
|
A:CU603
|
4.4
|
6.5
|
0.8
|
HD2
|
A:HIS65
|
4.5
|
6.2
|
1.0
|
CG
|
A:PHE450
|
4.5
|
7.0
|
1.0
|
HB2
|
A:PHE450
|
4.5
|
6.7
|
1.0
|
CD2
|
A:HIS65
|
4.6
|
6.1
|
1.0
|
HE2
|
A:PHE450
|
4.7
|
8.0
|
1.0
|
NE2
|
A:HIS65
|
4.7
|
6.4
|
1.0
|
CE2
|
A:PHE450
|
4.7
|
8.1
|
1.0
|
HD1
|
A:HIS402
|
4.8
|
6.0
|
1.0
|
O2
|
A:OXY610
|
4.8
|
13.7
|
0.5
|
NE2
|
A:HIS400
|
4.8
|
6.1
|
1.0
|
HD1
|
A:HIS452
|
4.8
|
8.0
|
1.0
|
HD1
|
A:HIS112
|
4.8
|
7.0
|
1.0
|
CU
|
A:CU602
|
4.8
|
11.4
|
0.5
|
CB
|
A:PRO80
|
5.0
|
6.1
|
1.0
|
HD22
|
A:LEU459
|
5.0
|
8.7
|
1.0
|
|
Copper binding site 3 out
of 6 in 5mhy
Go back to
Copper Binding Sites List in 5mhy
Copper binding site 3 out
of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:11.4
occ:0.45
|
CU
|
A:CU602
|
0.0
|
11.4
|
0.5
|
CU
|
A:CU602
|
0.6
|
4.5
|
0.5
|
NE2
|
A:HIS454
|
2.1
|
6.9
|
1.0
|
ND1
|
A:HIS67
|
2.1
|
6.4
|
1.0
|
NE2
|
A:HIS110
|
2.1
|
6.7
|
1.0
|
O
|
A:HOH701
|
2.2
|
9.0
|
0.4
|
O1
|
A:OXY609
|
2.2
|
6.8
|
0.4
|
O
|
A:HOH705
|
2.3
|
10.3
|
0.4
|
O
|
A:HOH704
|
2.5
|
3.6
|
0.2
|
O2
|
A:OXY609
|
2.8
|
9.4
|
0.4
|
HD2
|
A:HIS65
|
2.8
|
6.2
|
1.0
|
CE1
|
A:HIS110
|
3.0
|
6.9
|
1.0
|
CE1
|
A:HIS67
|
3.0
|
6.1
|
1.0
|
HB2
|
A:HIS67
|
3.0
|
5.8
|
1.0
|
HE1
|
A:HIS110
|
3.0
|
6.7
|
1.0
|
CE1
|
A:HIS454
|
3.1
|
6.9
|
1.0
|
CD2
|
A:HIS454
|
3.1
|
6.7
|
1.0
|
HE1
|
A:HIS67
|
3.1
|
6.2
|
1.0
|
CG
|
A:HIS67
|
3.2
|
5.8
|
1.0
|
HD2
|
A:HIS454
|
3.2
|
6.6
|
1.0
|
CD2
|
A:HIS110
|
3.2
|
6.3
|
1.0
|
HE1
|
A:HIS454
|
3.3
|
6.8
|
1.0
|
HD2
|
A:HIS110
|
3.5
|
6.3
|
1.0
|
CB
|
A:HIS67
|
3.6
|
5.8
|
1.0
|
CD2
|
A:HIS65
|
3.6
|
6.1
|
1.0
|
CU
|
A:CU603
|
3.7
|
6.5
|
0.8
|
HD2
|
A:HIS400
|
3.9
|
6.2
|
1.0
|
HZ2
|
A:TRP108
|
3.9
|
5.9
|
1.0
|
HB2
|
A:ALA244
|
3.9
|
5.3
|
1.0
|
NE2
|
A:HIS65
|
4.1
|
6.4
|
1.0
|
CD2
|
A:HIS400
|
4.1
|
6.2
|
1.0
|
NE2
|
A:HIS400
|
4.1
|
6.1
|
1.0
|
O
|
A:HOH702
|
4.1
|
13.5
|
0.5
|
CU
|
A:CU601
|
4.1
|
7.4
|
0.5
|
NE2
|
A:HIS67
|
4.1
|
6.3
|
1.0
|
ND1
|
A:HIS110
|
4.2
|
6.3
|
1.0
|
ND1
|
A:HIS454
|
4.2
|
6.4
|
1.0
|
CG
|
A:HIS454
|
4.2
|
6.2
|
1.0
|
CZ2
|
A:TRP108
|
4.2
|
6.0
|
1.0
|
HB3
|
A:HIS67
|
4.3
|
5.8
|
1.0
|
CD2
|
A:HIS67
|
4.3
|
6.6
|
1.0
|
HA
|
A:HIS67
|
4.3
|
5.7
|
1.0
|
CG
|
A:HIS110
|
4.3
|
6.1
|
1.0
|
HE1
|
A:TRP108
|
4.4
|
5.6
|
1.0
|
CE2
|
A:TRP108
|
4.5
|
5.7
|
1.0
|
HD2
|
A:HIS112
|
4.6
|
6.8
|
1.0
|
HB1
|
A:ALA244
|
4.6
|
5.3
|
1.0
|
HE1
|
A:HIS452
|
4.6
|
8.8
|
1.0
|
CA
|
A:HIS67
|
4.6
|
5.7
|
1.0
|
NE1
|
A:TRP108
|
4.6
|
5.5
|
1.0
|
CB
|
A:ALA244
|
4.7
|
5.3
|
1.0
|
O1
|
A:OXY610
|
4.7
|
12.3
|
0.5
|
CU
|
A:CU601
|
4.8
|
5.5
|
0.5
|
CG
|
A:HIS65
|
4.9
|
6.2
|
1.0
|
HD1
|
A:HIS110
|
4.9
|
6.4
|
1.0
|
HE2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
CG
|
A:HIS400
|
4.9
|
6.1
|
1.0
|
HD1
|
A:HIS454
|
5.0
|
6.5
|
1.0
|
CH2
|
A:TRP108
|
5.0
|
6.1
|
1.0
|
CE1
|
A:HIS400
|
5.0
|
6.3
|
1.0
|
|
Copper binding site 4 out
of 6 in 5mhy
Go back to
Copper Binding Sites List in 5mhy
Copper binding site 4 out
of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:4.5
occ:0.45
|
CU
|
A:CU602
|
0.0
|
4.5
|
0.5
|
CU
|
A:CU602
|
0.6
|
11.4
|
0.5
|
ND1
|
A:HIS67
|
1.9
|
6.4
|
1.0
|
NE2
|
A:HIS110
|
2.0
|
6.7
|
1.0
|
NE2
|
A:HIS454
|
2.1
|
6.9
|
1.0
|
O
|
A:HOH701
|
2.7
|
9.0
|
0.4
|
O1
|
A:OXY609
|
2.8
|
6.8
|
0.4
|
HB2
|
A:HIS67
|
2.8
|
5.8
|
1.0
|
O
|
A:HOH705
|
2.8
|
10.3
|
0.4
|
CE1
|
A:HIS67
|
2.9
|
6.1
|
1.0
|
CD2
|
A:HIS110
|
2.9
|
6.3
|
1.0
|
CE1
|
A:HIS454
|
3.0
|
6.9
|
1.0
|
CG
|
A:HIS67
|
3.0
|
5.8
|
1.0
|
CE1
|
A:HIS110
|
3.0
|
6.9
|
1.0
|
O
|
A:HOH704
|
3.1
|
3.6
|
0.2
|
HE1
|
A:HIS454
|
3.1
|
6.8
|
1.0
|
HE1
|
A:HIS67
|
3.1
|
6.2
|
1.0
|
HD2
|
A:HIS110
|
3.1
|
6.3
|
1.0
|
HD2
|
A:HIS65
|
3.1
|
6.2
|
1.0
|
CD2
|
A:HIS454
|
3.2
|
6.7
|
1.0
|
HE1
|
A:HIS110
|
3.3
|
6.7
|
1.0
|
O2
|
A:OXY609
|
3.3
|
9.4
|
0.4
|
CB
|
A:HIS67
|
3.4
|
5.8
|
1.0
|
HD2
|
A:HIS454
|
3.4
|
6.6
|
1.0
|
HZ2
|
A:TRP108
|
3.4
|
5.9
|
1.0
|
HB2
|
A:ALA244
|
3.6
|
5.3
|
1.0
|
CZ2
|
A:TRP108
|
3.7
|
6.0
|
1.0
|
HE1
|
A:TRP108
|
3.9
|
5.6
|
1.0
|
HB3
|
A:HIS67
|
3.9
|
5.8
|
1.0
|
CD2
|
A:HIS65
|
3.9
|
6.1
|
1.0
|
CE2
|
A:TRP108
|
3.9
|
5.7
|
1.0
|
NE2
|
A:HIS67
|
4.0
|
6.3
|
1.0
|
CD2
|
A:HIS67
|
4.1
|
6.6
|
1.0
|
NE1
|
A:TRP108
|
4.1
|
5.5
|
1.0
|
CU
|
A:CU603
|
4.1
|
6.5
|
0.8
|
ND1
|
A:HIS454
|
4.1
|
6.4
|
1.0
|
ND1
|
A:HIS110
|
4.1
|
6.3
|
1.0
|
CG
|
A:HIS110
|
4.1
|
6.1
|
1.0
|
CG
|
A:HIS454
|
4.3
|
6.2
|
1.0
|
HB1
|
A:ALA244
|
4.3
|
5.3
|
1.0
|
HD2
|
A:HIS400
|
4.3
|
6.2
|
1.0
|
CB
|
A:ALA244
|
4.3
|
5.3
|
1.0
|
HA
|
A:HIS67
|
4.4
|
5.7
|
1.0
|
O
|
A:HOH702
|
4.4
|
13.5
|
0.5
|
NE2
|
A:HIS65
|
4.4
|
6.4
|
1.0
|
NE2
|
A:HIS400
|
4.5
|
6.1
|
1.0
|
CH2
|
A:TRP108
|
4.5
|
6.1
|
1.0
|
CD2
|
A:HIS400
|
4.5
|
6.2
|
1.0
|
CA
|
A:HIS67
|
4.5
|
5.7
|
1.0
|
HH2
|
A:TRP108
|
4.6
|
6.0
|
1.0
|
CU
|
A:CU601
|
4.7
|
7.4
|
0.5
|
HB3
|
A:ALA244
|
4.8
|
5.2
|
1.0
|
HE2
|
A:HIS67
|
4.8
|
6.3
|
1.0
|
CD2
|
A:TRP108
|
4.8
|
5.4
|
1.0
|
HD1
|
A:HIS454
|
4.9
|
6.5
|
1.0
|
HD1
|
A:HIS110
|
4.9
|
6.4
|
1.0
|
HD2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
O1
|
A:OXY610
|
5.0
|
12.3
|
0.5
|
HD2
|
A:HIS112
|
5.0
|
6.8
|
1.0
|
|
Copper binding site 5 out
of 6 in 5mhy
Go back to
Copper Binding Sites List in 5mhy
Copper binding site 5 out
of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:6.5
occ:0.80
|
NE2
|
A:HIS400
|
1.9
|
6.1
|
1.0
|
NE2
|
A:HIS65
|
1.9
|
6.4
|
1.0
|
O
|
A:HOH705
|
1.9
|
10.3
|
0.4
|
O
|
A:HOH1004
|
2.1
|
4.6
|
0.4
|
O
|
A:HOH1078
|
2.8
|
5.5
|
0.6
|
CE1
|
A:HIS65
|
2.9
|
6.3
|
1.0
|
CD2
|
A:HIS400
|
2.9
|
6.2
|
1.0
|
CE1
|
A:HIS400
|
2.9
|
6.3
|
1.0
|
CD2
|
A:HIS65
|
2.9
|
6.1
|
1.0
|
HD2
|
A:HIS400
|
3.1
|
6.2
|
1.0
|
HA
|
A:HIS67
|
3.1
|
5.7
|
1.0
|
HE1
|
A:HIS65
|
3.1
|
6.3
|
1.0
|
O1
|
A:OXY609
|
3.1
|
6.8
|
0.4
|
HE1
|
A:HIS400
|
3.1
|
6.1
|
1.0
|
HD2
|
A:HIS65
|
3.1
|
6.2
|
1.0
|
O
|
A:HOH704
|
3.2
|
3.6
|
0.2
|
H
|
A:GLY68
|
3.3
|
5.7
|
1.0
|
CD2
|
A:HIS402
|
3.4
|
5.9
|
1.0
|
NE2
|
A:HIS402
|
3.5
|
6.1
|
1.0
|
ND1
|
A:HIS67
|
3.5
|
6.4
|
1.0
|
HD2
|
A:HIS402
|
3.6
|
6.0
|
1.0
|
O
|
A:HOH701
|
3.7
|
9.0
|
0.4
|
CU
|
A:CU602
|
3.7
|
11.4
|
0.5
|
HA
|
A:HIS402
|
3.7
|
6.0
|
1.0
|
CG
|
A:HIS402
|
3.8
|
5.9
|
1.0
|
CG
|
A:HIS67
|
3.8
|
5.8
|
1.0
|
CE1
|
A:HIS402
|
3.8
|
6.2
|
1.0
|
CU
|
A:CU601
|
3.9
|
7.4
|
0.5
|
CE1
|
A:HIS67
|
3.9
|
6.1
|
1.0
|
CA
|
A:HIS67
|
3.9
|
5.7
|
1.0
|
ND1
|
A:HIS402
|
4.0
|
5.9
|
1.0
|
ND1
|
A:HIS65
|
4.0
|
6.4
|
1.0
|
ND1
|
A:HIS400
|
4.0
|
5.9
|
1.0
|
CG
|
A:HIS400
|
4.0
|
6.1
|
1.0
|
CG
|
A:HIS65
|
4.0
|
6.2
|
1.0
|
CU
|
A:CU602
|
4.1
|
4.5
|
0.5
|
N
|
A:GLY68
|
4.1
|
5.5
|
1.0
|
HB2
|
A:HIS67
|
4.1
|
5.8
|
1.0
|
CB
|
A:HIS67
|
4.2
|
5.8
|
1.0
|
HE1
|
A:HIS67
|
4.2
|
6.2
|
1.0
|
HE1
|
A:HIS402
|
4.3
|
6.1
|
1.0
|
O2
|
A:OXY609
|
4.3
|
9.4
|
0.4
|
CD2
|
A:HIS67
|
4.4
|
6.6
|
1.0
|
NE2
|
A:HIS67
|
4.4
|
6.3
|
1.0
|
CU
|
A:CU601
|
4.4
|
5.5
|
0.5
|
CA
|
A:HIS402
|
4.5
|
6.0
|
1.0
|
HD1
|
A:HIS402
|
4.5
|
6.0
|
1.0
|
C
|
A:HIS67
|
4.6
|
5.8
|
1.0
|
CB
|
A:HIS402
|
4.6
|
6.2
|
1.0
|
O
|
A:HOH945
|
4.7
|
10.8
|
1.0
|
HD1
|
A:HIS65
|
4.8
|
6.3
|
1.0
|
HB3
|
A:HIS402
|
4.8
|
6.1
|
1.0
|
HD1
|
A:HIS400
|
4.8
|
6.0
|
1.0
|
O
|
A:HOH852
|
4.8
|
9.3
|
1.0
|
N
|
A:HIS402
|
4.9
|
5.9
|
1.0
|
HD2
|
A:HIS112
|
4.9
|
6.8
|
1.0
|
HD2
|
A:HIS454
|
4.9
|
6.6
|
1.0
|
HA2
|
A:GLY68
|
4.9
|
5.8
|
1.0
|
HD2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
HE2
|
A:HIS67
|
5.0
|
6.3
|
1.0
|
N
|
A:HIS67
|
5.0
|
5.4
|
1.0
|
|
Copper binding site 6 out
of 6 in 5mhy
Go back to
Copper Binding Sites List in 5mhy
Copper binding site 6 out
of 6 in the The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the Seventh Structure of the Series with Total Exposition Time 183 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu604
b:6.0
occ:0.90
|
ND1
|
A:HIS458
|
2.0
|
6.6
|
1.0
|
ND1
|
A:HIS397
|
2.0
|
6.8
|
1.0
|
SG
|
A:CYS453
|
2.2
|
6.7
|
1.0
|
HD11
|
A:ILE455
|
2.7
|
6.3
|
1.0
|
CE1
|
A:HIS397
|
3.0
|
6.8
|
1.0
|
CE1
|
A:HIS458
|
3.0
|
7.0
|
1.0
|
HB
|
A:ILE455
|
3.0
|
6.4
|
1.0
|
HD2
|
A:PHE463
|
3.0
|
6.2
|
1.0
|
CG
|
A:HIS458
|
3.1
|
6.7
|
1.0
|
HB3
|
A:HIS397
|
3.1
|
6.4
|
1.0
|
CG
|
A:HIS397
|
3.1
|
6.3
|
1.0
|
HE1
|
A:HIS397
|
3.1
|
6.9
|
1.0
|
HB2
|
A:HIS458
|
3.1
|
7.1
|
1.0
|
HE1
|
A:HIS458
|
3.2
|
7.0
|
1.0
|
HB3
|
A:HIS458
|
3.3
|
7.1
|
1.0
|
CB
|
A:CYS453
|
3.3
|
6.7
|
1.0
|
HB2
|
A:CYS453
|
3.4
|
6.6
|
1.0
|
CB
|
A:HIS458
|
3.4
|
7.1
|
1.0
|
HA
|
A:HIS397
|
3.4
|
6.3
|
1.0
|
HB3
|
A:CYS453
|
3.4
|
6.6
|
1.0
|
CB
|
A:HIS397
|
3.5
|
6.5
|
1.0
|
HE2
|
A:PHE463
|
3.5
|
6.3
|
1.0
|
CD1
|
A:ILE455
|
3.6
|
6.3
|
1.0
|
HD2
|
A:PRO398
|
3.8
|
6.0
|
1.0
|
CD2
|
A:PHE463
|
3.8
|
6.0
|
1.0
|
CB
|
A:ILE455
|
3.9
|
6.3
|
1.0
|
H
|
A:ILE455
|
3.9
|
6.7
|
1.0
|
HD12
|
A:ILE455
|
3.9
|
6.3
|
1.0
|
CA
|
A:HIS397
|
4.0
|
6.3
|
1.0
|
CE2
|
A:PHE463
|
4.0
|
6.4
|
1.0
|
CG1
|
A:ILE455
|
4.1
|
6.3
|
1.0
|
HG13
|
A:ILE455
|
4.1
|
6.3
|
1.0
|
NE2
|
A:HIS397
|
4.1
|
7.4
|
1.0
|
NE2
|
A:HIS458
|
4.1
|
7.5
|
1.0
|
CD2
|
A:HIS458
|
4.2
|
6.6
|
1.0
|
CD2
|
A:HIS397
|
4.2
|
6.9
|
1.0
|
HD13
|
A:ILE455
|
4.2
|
6.3
|
1.0
|
HB2
|
A:HIS397
|
4.4
|
6.4
|
1.0
|
HG21
|
A:ILE455
|
4.6
|
6.6
|
1.0
|
HZ
|
A:PHE341
|
4.6
|
7.8
|
1.0
|
O
|
A:GLY394
|
4.6
|
9.5
|
1.0
|
HG22
|
A:ILE455
|
4.6
|
6.5
|
1.0
|
CD
|
A:PRO398
|
4.6
|
6.1
|
1.0
|
CG2
|
A:ILE455
|
4.7
|
6.7
|
1.0
|
CA
|
A:CYS453
|
4.7
|
6.2
|
1.0
|
CZ
|
A:PHE341
|
4.8
|
7.8
|
1.0
|
N
|
A:ILE455
|
4.8
|
6.7
|
1.0
|
HE1
|
A:PHE399
|
4.8
|
7.3
|
1.0
|
HA
|
A:CYS453
|
4.8
|
6.3
|
1.0
|
HD3
|
A:PRO398
|
4.9
|
6.0
|
1.0
|
HE2
|
A:PHE341
|
4.9
|
7.8
|
1.0
|
HE2
|
A:HIS397
|
4.9
|
7.1
|
1.0
|
CA
|
A:HIS458
|
4.9
|
7.5
|
1.0
|
HE2
|
A:HIS458
|
4.9
|
7.2
|
1.0
|
CA
|
A:ILE455
|
4.9
|
6.5
|
1.0
|
CE2
|
A:PHE341
|
4.9
|
7.7
|
1.0
|
C
|
A:HIS397
|
5.0
|
6.1
|
1.0
|
O
|
A:ILE455
|
5.0
|
6.7
|
1.0
|
HB3
|
A:PHE463
|
5.0
|
6.4
|
1.0
|
N
|
A:HIS397
|
5.0
|
6.3
|
1.0
|
|
Reference:
K.M.Polyakov,
S.Gavryushov,
S.Ivanova,
T.V.Fedorova,
O.A.Glazunova,
A.N.Popov,
O.V.Koroleva.
Structural Study of the X-Ray-Induced Enzymatic Reduction of Molecular Oxygen to Water By Steccherinum Murashkinskyi Laccase: Insights Into the Reaction Mechanism. Acta Crystallogr D Struct V. 73 388 2017BIOL.
ISSN: ISSN 2059-7983
PubMed: 28471364
DOI: 10.1107/S2059798317003667
Page generated: Wed Jul 31 04:31:41 2024
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