Copper in PDB 5mid: The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 Min.
Enzymatic activity of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 Min., PDB code: 5mid
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)
|
67.50 /
1.35
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.370,
84.390,
112.480,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
13.2 /
15
|
Other elements in 5mid:
The structure of The Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi.the 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 Min.
(pdb code 5mid). 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 14-Th Structure of the Series with Total Exposition Time 393 Min., PDB code: 5mid:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 5mid
Go back to
Copper Binding Sites List in 5mid
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 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:6.2
occ:0.20
|
CU
|
A:CU601
|
0.0
|
6.2
|
0.2
|
CU
|
A:CU601
|
0.7
|
6.8
|
0.7
|
O
|
A:HOH704
|
1.7
|
7.9
|
0.5
|
O
|
A:HOH702
|
1.8
|
8.9
|
0.2
|
O2
|
A:OXY609
|
2.0
|
3.8
|
0.2
|
NE2
|
A:HIS402
|
2.1
|
6.3
|
1.0
|
O1
|
A:OXY609
|
2.1
|
3.6
|
0.2
|
NE2
|
A:HIS452
|
2.2
|
8.1
|
1.0
|
NE2
|
A:HIS112
|
2.2
|
6.8
|
1.0
|
O
|
A:HOH705
|
2.5
|
5.2
|
0.2
|
CE1
|
A:HIS402
|
3.0
|
6.2
|
1.0
|
HD2
|
A:HIS400
|
3.0
|
6.2
|
1.0
|
CE1
|
A:HIS452
|
3.0
|
8.7
|
1.0
|
CD2
|
A:HIS112
|
3.1
|
6.7
|
1.0
|
HE1
|
A:HIS402
|
3.1
|
6.2
|
1.0
|
HE1
|
A:HIS452
|
3.1
|
8.2
|
1.0
|
HD2
|
A:HIS112
|
3.1
|
6.7
|
1.0
|
CD2
|
A:HIS402
|
3.2
|
6.2
|
1.0
|
CE1
|
A:HIS112
|
3.3
|
7.4
|
1.0
|
CD2
|
A:HIS452
|
3.3
|
7.4
|
1.0
|
HD2
|
A:HIS402
|
3.4
|
6.2
|
1.0
|
HE1
|
A:HIS112
|
3.5
|
7.2
|
1.0
|
O
|
A:HOH701
|
3.6
|
10.8
|
0.5
|
HD2
|
A:HIS452
|
3.6
|
7.5
|
1.0
|
CD2
|
A:HIS400
|
3.8
|
6.3
|
1.0
|
HD2
|
A:PHE450
|
3.9
|
8.1
|
1.0
|
HE1
|
A:HIS110
|
3.9
|
6.5
|
1.0
|
CU
|
A:CU603
|
3.9
|
6.5
|
0.8
|
HD2
|
A:HIS65
|
3.9
|
6.3
|
1.0
|
O1
|
A:OXY610
|
4.1
|
17.9
|
0.5
|
CD2
|
A:HIS65
|
4.1
|
6.3
|
1.0
|
ND1
|
A:HIS402
|
4.1
|
6.2
|
1.0
|
CU
|
A:CU602
|
4.1
|
6.1
|
0.2
|
HB3
|
A:PHE450
|
4.1
|
6.8
|
1.0
|
NE2
|
A:HIS65
|
4.2
|
6.6
|
1.0
|
ND1
|
A:HIS452
|
4.2
|
7.4
|
1.0
|
CG
|
A:HIS402
|
4.2
|
6.0
|
1.0
|
CG
|
A:HIS112
|
4.3
|
6.7
|
1.0
|
NE2
|
A:HIS400
|
4.3
|
6.4
|
1.0
|
ND1
|
A:HIS112
|
4.3
|
7.1
|
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
|
8.2
|
1.0
|
HD2
|
A:HIS454
|
4.6
|
6.8
|
1.0
|
CU
|
A:CU602
|
4.7
|
5.9
|
0.7
|
NE2
|
A:HIS454
|
4.7
|
7.1
|
1.0
|
CE1
|
A:HIS110
|
4.7
|
6.7
|
1.0
|
HD21
|
A:LEU459
|
4.7
|
8.6
|
1.0
|
O2
|
A:OXY610
|
4.8
|
17.2
|
0.5
|
CD2
|
A:HIS454
|
4.8
|
6.8
|
1.0
|
CG
|
A:HIS65
|
4.8
|
6.1
|
1.0
|
HD1
|
A:HIS402
|
4.9
|
6.1
|
1.0
|
CE1
|
A:HIS65
|
4.9
|
6.2
|
1.0
|
CB
|
A:PHE450
|
5.0
|
6.9
|
1.0
|
HD1
|
A:HIS452
|
5.0
|
7.6
|
1.0
|
|
Copper binding site 2 out
of 6 in 5mid
Go back to
Copper Binding Sites List in 5mid
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 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu601
b:6.8
occ:0.70
|
CU
|
A:CU601
|
0.0
|
6.8
|
0.7
|
CU
|
A:CU601
|
0.7
|
6.2
|
0.2
|
NE2
|
A:HIS452
|
1.9
|
8.1
|
1.0
|
NE2
|
A:HIS402
|
2.0
|
6.3
|
1.0
|
NE2
|
A:HIS112
|
2.0
|
6.8
|
1.0
|
O
|
A:HOH704
|
2.4
|
7.9
|
0.5
|
O
|
A:HOH702
|
2.4
|
8.9
|
0.2
|
O2
|
A:OXY609
|
2.5
|
3.8
|
0.2
|
O1
|
A:OXY609
|
2.8
|
3.6
|
0.2
|
CE1
|
A:HIS402
|
2.9
|
6.2
|
1.0
|
CD2
|
A:HIS452
|
2.9
|
7.4
|
1.0
|
CE1
|
A:HIS112
|
3.0
|
7.4
|
1.0
|
CE1
|
A:HIS452
|
3.0
|
8.7
|
1.0
|
HE1
|
A:HIS402
|
3.0
|
6.2
|
1.0
|
HD2
|
A:HIS452
|
3.1
|
7.5
|
1.0
|
CD2
|
A:HIS402
|
3.1
|
6.2
|
1.0
|
HE1
|
A:HIS112
|
3.1
|
7.2
|
1.0
|
CD2
|
A:HIS112
|
3.1
|
6.7
|
1.0
|
O
|
A:HOH705
|
3.1
|
5.2
|
0.2
|
HE1
|
A:HIS452
|
3.2
|
8.2
|
1.0
|
HD2
|
A:PHE450
|
3.3
|
8.1
|
1.0
|
HD2
|
A:HIS402
|
3.3
|
6.2
|
1.0
|
HD2
|
A:HIS400
|
3.3
|
6.2
|
1.0
|
HD2
|
A:HIS112
|
3.3
|
6.7
|
1.0
|
HB3
|
A:PHE450
|
3.6
|
6.8
|
1.0
|
O
|
A:HOH701
|
3.8
|
10.8
|
0.5
|
CD2
|
A:PHE450
|
3.9
|
8.2
|
1.0
|
ND1
|
A:HIS402
|
4.0
|
6.2
|
1.0
|
HB3
|
A:PRO80
|
4.0
|
6.2
|
1.0
|
ND1
|
A:HIS452
|
4.1
|
7.4
|
1.0
|
CG
|
A:HIS452
|
4.1
|
7.0
|
1.0
|
ND1
|
A:HIS112
|
4.1
|
7.1
|
1.0
|
CG
|
A:HIS402
|
4.2
|
6.0
|
1.0
|
CD2
|
A:HIS400
|
4.2
|
6.3
|
1.0
|
CG
|
A:HIS112
|
4.2
|
6.7
|
1.0
|
O1
|
A:OXY610
|
4.3
|
17.9
|
0.5
|
HE1
|
A:HIS110
|
4.4
|
6.5
|
1.0
|
CU
|
A:CU603
|
4.4
|
6.5
|
0.8
|
CB
|
A:PHE450
|
4.4
|
6.9
|
1.0
|
HD21
|
A:LEU459
|
4.4
|
8.6
|
1.0
|
HD2
|
A:HIS65
|
4.5
|
6.3
|
1.0
|
HB2
|
A:PHE450
|
4.5
|
6.8
|
1.0
|
CD2
|
A:HIS65
|
4.6
|
6.3
|
1.0
|
CG
|
A:PHE450
|
4.6
|
7.0
|
1.0
|
NE2
|
A:HIS65
|
4.6
|
6.6
|
1.0
|
HE2
|
A:PHE450
|
4.7
|
8.7
|
1.0
|
CE2
|
A:PHE450
|
4.8
|
8.8
|
1.0
|
NE2
|
A:HIS400
|
4.8
|
6.4
|
1.0
|
CU
|
A:CU602
|
4.8
|
6.1
|
0.2
|
HD1
|
A:HIS402
|
4.8
|
6.1
|
1.0
|
HD1
|
A:HIS452
|
4.9
|
7.6
|
1.0
|
O2
|
A:OXY610
|
4.9
|
17.2
|
0.5
|
HD1
|
A:HIS112
|
4.9
|
7.0
|
1.0
|
HD22
|
A:LEU459
|
5.0
|
8.6
|
1.0
|
CB
|
A:PRO80
|
5.0
|
6.2
|
1.0
|
|
Copper binding site 3 out
of 6 in 5mid
Go back to
Copper Binding Sites List in 5mid
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 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:6.1
occ:0.20
|
CU
|
A:CU602
|
0.0
|
6.1
|
0.2
|
CU
|
A:CU602
|
0.6
|
5.9
|
0.7
|
O1
|
A:OXY609
|
2.0
|
3.6
|
0.2
|
NE2
|
A:HIS454
|
2.0
|
7.1
|
1.0
|
NE2
|
A:HIS110
|
2.1
|
6.6
|
1.0
|
ND1
|
A:HIS67
|
2.1
|
6.3
|
1.0
|
O
|
A:HOH705
|
2.3
|
5.2
|
0.2
|
O
|
A:HOH702
|
2.4
|
8.9
|
0.2
|
O
|
A:HOH704
|
2.4
|
7.9
|
0.5
|
O2
|
A:OXY609
|
2.7
|
3.8
|
0.2
|
HD2
|
A:HIS65
|
2.8
|
6.3
|
1.0
|
CE1
|
A:HIS110
|
2.9
|
6.7
|
1.0
|
HE1
|
A:HIS110
|
3.0
|
6.5
|
1.0
|
HB2
|
A:HIS67
|
3.0
|
5.7
|
1.0
|
CE1
|
A:HIS454
|
3.0
|
7.5
|
1.0
|
CE1
|
A:HIS67
|
3.1
|
6.2
|
1.0
|
CD2
|
A:HIS454
|
3.1
|
6.8
|
1.0
|
HE1
|
A:HIS67
|
3.2
|
6.2
|
1.0
|
HE1
|
A:HIS454
|
3.2
|
7.2
|
1.0
|
HD2
|
A:HIS454
|
3.2
|
6.8
|
1.0
|
CG
|
A:HIS67
|
3.2
|
5.8
|
1.0
|
CD2
|
A:HIS110
|
3.3
|
6.0
|
1.0
|
HD2
|
A:HIS110
|
3.5
|
6.2
|
1.0
|
CD2
|
A:HIS65
|
3.6
|
6.3
|
1.0
|
CB
|
A:HIS67
|
3.6
|
5.7
|
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
|
6.0
|
1.0
|
HB2
|
A:ALA244
|
4.0
|
5.4
|
1.0
|
O
|
A:HOH701
|
4.1
|
10.8
|
0.5
|
NE2
|
A:HIS65
|
4.1
|
6.6
|
1.0
|
CD2
|
A:HIS400
|
4.1
|
6.3
|
1.0
|
ND1
|
A:HIS110
|
4.1
|
6.3
|
1.0
|
CU
|
A:CU601
|
4.1
|
6.2
|
0.2
|
NE2
|
A:HIS400
|
4.1
|
6.4
|
1.0
|
ND1
|
A:HIS454
|
4.2
|
7.0
|
1.0
|
CG
|
A:HIS454
|
4.2
|
6.6
|
1.0
|
NE2
|
A:HIS67
|
4.2
|
6.2
|
1.0
|
CZ2
|
A:TRP108
|
4.2
|
6.1
|
1.0
|
HB3
|
A:HIS67
|
4.3
|
5.7
|
1.0
|
CG
|
A:HIS110
|
4.3
|
6.1
|
1.0
|
CD2
|
A:HIS67
|
4.3
|
6.6
|
1.0
|
HA
|
A:HIS67
|
4.3
|
5.7
|
1.0
|
HE1
|
A:TRP108
|
4.5
|
6.1
|
1.0
|
CE2
|
A:TRP108
|
4.5
|
5.8
|
1.0
|
HD2
|
A:HIS112
|
4.6
|
6.7
|
1.0
|
HB1
|
A:ALA244
|
4.6
|
5.4
|
1.0
|
HE1
|
A:HIS452
|
4.6
|
8.2
|
1.0
|
NE1
|
A:TRP108
|
4.6
|
6.0
|
1.0
|
CA
|
A:HIS67
|
4.6
|
5.7
|
1.0
|
CB
|
A:ALA244
|
4.7
|
5.5
|
1.0
|
O1
|
A:OXY610
|
4.7
|
17.9
|
0.5
|
CU
|
A:CU601
|
4.8
|
6.8
|
0.7
|
HD1
|
A:HIS110
|
4.8
|
6.3
|
1.0
|
CG
|
A:HIS65
|
4.8
|
6.1
|
1.0
|
CH2
|
A:TRP108
|
4.9
|
6.3
|
1.0
|
HD1
|
A:HIS454
|
4.9
|
7.0
|
1.0
|
CG
|
A:HIS400
|
5.0
|
5.8
|
1.0
|
HE2
|
A:HIS67
|
5.0
|
6.3
|
1.0
|
HB3
|
A:HIS65
|
5.0
|
6.2
|
1.0
|
|
Copper binding site 4 out
of 6 in 5mid
Go back to
Copper Binding Sites List in 5mid
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 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu602
b:5.9
occ:0.70
|
CU
|
A:CU602
|
0.0
|
5.9
|
0.7
|
CU
|
A:CU602
|
0.6
|
6.1
|
0.2
|
ND1
|
A:HIS67
|
1.9
|
6.3
|
1.0
|
NE2
|
A:HIS110
|
2.0
|
6.6
|
1.0
|
NE2
|
A:HIS454
|
2.1
|
7.1
|
1.0
|
O1
|
A:OXY609
|
2.5
|
3.6
|
0.2
|
HB2
|
A:HIS67
|
2.8
|
5.7
|
1.0
|
O
|
A:HOH705
|
2.8
|
5.2
|
0.2
|
O
|
A:HOH702
|
2.9
|
8.9
|
0.2
|
CE1
|
A:HIS67
|
2.9
|
6.2
|
1.0
|
O
|
A:HOH704
|
2.9
|
7.9
|
0.5
|
CG
|
A:HIS67
|
3.0
|
5.8
|
1.0
|
CE1
|
A:HIS454
|
3.0
|
7.5
|
1.0
|
CD2
|
A:HIS110
|
3.0
|
6.0
|
1.0
|
CE1
|
A:HIS110
|
3.0
|
6.7
|
1.0
|
HD2
|
A:HIS65
|
3.1
|
6.3
|
1.0
|
HE1
|
A:HIS67
|
3.1
|
6.2
|
1.0
|
HE1
|
A:HIS454
|
3.1
|
7.2
|
1.0
|
HD2
|
A:HIS110
|
3.2
|
6.2
|
1.0
|
CD2
|
A:HIS454
|
3.2
|
6.8
|
1.0
|
O2
|
A:OXY609
|
3.2
|
3.8
|
0.2
|
HE1
|
A:HIS110
|
3.2
|
6.5
|
1.0
|
CB
|
A:HIS67
|
3.4
|
5.7
|
1.0
|
HD2
|
A:HIS454
|
3.4
|
6.8
|
1.0
|
HZ2
|
A:TRP108
|
3.5
|
6.0
|
1.0
|
HB2
|
A:ALA244
|
3.6
|
5.4
|
1.0
|
CZ2
|
A:TRP108
|
3.7
|
6.1
|
1.0
|
CD2
|
A:HIS65
|
3.9
|
6.3
|
1.0
|
HB3
|
A:HIS67
|
3.9
|
5.7
|
1.0
|
HE1
|
A:TRP108
|
3.9
|
6.1
|
1.0
|
CE2
|
A:TRP108
|
4.0
|
5.8
|
1.0
|
NE2
|
A:HIS67
|
4.0
|
6.2
|
1.0
|
CU
|
A:CU603
|
4.1
|
6.5
|
0.8
|
CD2
|
A:HIS67
|
4.1
|
6.6
|
1.0
|
NE1
|
A:TRP108
|
4.1
|
6.0
|
1.0
|
ND1
|
A:HIS110
|
4.1
|
6.3
|
1.0
|
CG
|
A:HIS110
|
4.1
|
6.1
|
1.0
|
ND1
|
A:HIS454
|
4.2
|
7.0
|
1.0
|
CG
|
A:HIS454
|
4.3
|
6.6
|
1.0
|
HD2
|
A:HIS400
|
4.3
|
6.2
|
1.0
|
HA
|
A:HIS67
|
4.3
|
5.7
|
1.0
|
HB1
|
A:ALA244
|
4.4
|
5.4
|
1.0
|
NE2
|
A:HIS65
|
4.4
|
6.6
|
1.0
|
CB
|
A:ALA244
|
4.4
|
5.5
|
1.0
|
O
|
A:HOH701
|
4.4
|
10.8
|
0.5
|
NE2
|
A:HIS400
|
4.4
|
6.4
|
1.0
|
CD2
|
A:HIS400
|
4.4
|
6.3
|
1.0
|
CA
|
A:HIS67
|
4.5
|
5.7
|
1.0
|
CH2
|
A:TRP108
|
4.5
|
6.3
|
1.0
|
CU
|
A:CU601
|
4.7
|
6.2
|
0.2
|
HH2
|
A:TRP108
|
4.7
|
6.3
|
1.0
|
HE2
|
A:HIS67
|
4.8
|
6.3
|
1.0
|
HB3
|
A:ALA244
|
4.8
|
5.4
|
1.0
|
CD2
|
A:TRP108
|
4.9
|
5.8
|
1.0
|
HD1
|
A:HIS110
|
4.9
|
6.3
|
1.0
|
HD1
|
A:HIS454
|
4.9
|
7.0
|
1.0
|
HD2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
HD2
|
A:HIS112
|
5.0
|
6.7
|
1.0
|
|
Copper binding site 5 out
of 6 in 5mid
Go back to
Copper Binding Sites List in 5mid
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 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:6.5
occ:0.80
|
NE2
|
A:HIS65
|
1.9
|
6.6
|
1.0
|
NE2
|
A:HIS400
|
1.9
|
6.4
|
1.0
|
O
|
A:HOH705
|
2.0
|
5.2
|
0.2
|
O
|
A:HOH955
|
2.0
|
2.7
|
0.2
|
O
|
A:HOH1103
|
2.8
|
6.1
|
0.8
|
CE1
|
A:HIS65
|
2.8
|
6.2
|
1.0
|
CD2
|
A:HIS400
|
2.8
|
6.3
|
1.0
|
CD2
|
A:HIS65
|
2.9
|
6.3
|
1.0
|
CE1
|
A:HIS400
|
2.9
|
6.2
|
1.0
|
HE1
|
A:HIS65
|
3.0
|
6.2
|
1.0
|
HD2
|
A:HIS400
|
3.0
|
6.2
|
1.0
|
HA
|
A:HIS67
|
3.1
|
5.7
|
1.0
|
HD2
|
A:HIS65
|
3.1
|
6.3
|
1.0
|
O1
|
A:OXY609
|
3.1
|
3.6
|
0.2
|
HE1
|
A:HIS400
|
3.1
|
6.1
|
1.0
|
O
|
A:HOH704
|
3.3
|
7.9
|
0.5
|
H
|
A:GLY68
|
3.3
|
5.7
|
1.0
|
O
|
A:HOH702
|
3.4
|
8.9
|
0.2
|
CD2
|
A:HIS402
|
3.4
|
6.2
|
1.0
|
NE2
|
A:HIS402
|
3.5
|
6.3
|
1.0
|
ND1
|
A:HIS67
|
3.5
|
6.3
|
1.0
|
HD2
|
A:HIS402
|
3.6
|
6.2
|
1.0
|
CU
|
A:CU602
|
3.7
|
6.1
|
0.2
|
HA
|
A:HIS402
|
3.7
|
6.0
|
1.0
|
CG
|
A:HIS402
|
3.8
|
6.0
|
1.0
|
CE1
|
A:HIS402
|
3.8
|
6.2
|
1.0
|
CG
|
A:HIS67
|
3.8
|
5.8
|
1.0
|
CU
|
A:CU601
|
3.9
|
6.2
|
0.2
|
CE1
|
A:HIS67
|
3.9
|
6.2
|
1.0
|
ND1
|
A:HIS65
|
4.0
|
6.0
|
1.0
|
ND1
|
A:HIS402
|
4.0
|
6.2
|
1.0
|
CA
|
A:HIS67
|
4.0
|
5.7
|
1.0
|
ND1
|
A:HIS400
|
4.0
|
5.7
|
1.0
|
CG
|
A:HIS400
|
4.0
|
5.8
|
1.0
|
CG
|
A:HIS65
|
4.0
|
6.1
|
1.0
|
CU
|
A:CU602
|
4.1
|
5.9
|
0.7
|
N
|
A:GLY68
|
4.1
|
5.5
|
1.0
|
HB2
|
A:HIS67
|
4.1
|
5.7
|
1.0
|
HE1
|
A:HIS67
|
4.2
|
6.2
|
1.0
|
CB
|
A:HIS67
|
4.2
|
5.7
|
1.0
|
HE1
|
A:HIS402
|
4.3
|
6.2
|
1.0
|
O2
|
A:OXY609
|
4.3
|
3.8
|
0.2
|
CU
|
A:CU601
|
4.4
|
6.8
|
0.7
|
CD2
|
A:HIS67
|
4.4
|
6.6
|
1.0
|
NE2
|
A:HIS67
|
4.4
|
6.2
|
1.0
|
HD1
|
A:HIS402
|
4.5
|
6.1
|
1.0
|
CA
|
A:HIS402
|
4.5
|
6.0
|
1.0
|
C
|
A:HIS67
|
4.6
|
5.7
|
1.0
|
CB
|
A:HIS402
|
4.6
|
6.1
|
1.0
|
O
|
A:HOH967
|
4.7
|
9.6
|
1.0
|
HD1
|
A:HIS65
|
4.7
|
6.1
|
1.0
|
HD1
|
A:HIS400
|
4.8
|
5.8
|
1.0
|
HB3
|
A:HIS402
|
4.8
|
6.1
|
1.0
|
O
|
A:HOH804
|
4.8
|
9.6
|
1.0
|
N
|
A:HIS402
|
4.9
|
6.0
|
1.0
|
HD2
|
A:HIS454
|
4.9
|
6.8
|
1.0
|
HA2
|
A:GLY68
|
4.9
|
5.9
|
1.0
|
HD2
|
A:HIS112
|
4.9
|
6.7
|
1.0
|
HD2
|
A:HIS67
|
5.0
|
6.3
|
1.0
|
HE2
|
A:HIS67
|
5.0
|
6.3
|
1.0
|
O
|
A:LEU401
|
5.0
|
6.3
|
1.0
|
|
Copper binding site 6 out
of 6 in 5mid
Go back to
Copper Binding Sites List in 5mid
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 14-Th Structure of the Series with Total Exposition Time 393 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 14-Th Structure of the Series with Total Exposition Time 393 Min. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu604
b:6.1
occ:0.90
|
ND1
|
A:HIS458
|
2.0
|
6.8
|
1.0
|
ND1
|
A:HIS397
|
2.0
|
6.9
|
1.0
|
SG
|
A:CYS453
|
2.2
|
6.8
|
1.0
|
HD11
|
A:ILE455
|
2.7
|
6.0
|
1.0
|
CE1
|
A:HIS397
|
3.0
|
6.9
|
1.0
|
CE1
|
A:HIS458
|
3.0
|
7.4
|
1.0
|
HB
|
A:ILE455
|
3.0
|
6.4
|
1.0
|
HD2
|
A:PHE463
|
3.1
|
6.5
|
1.0
|
CG
|
A:HIS458
|
3.1
|
6.9
|
1.0
|
HE1
|
A:HIS397
|
3.1
|
7.0
|
1.0
|
HB3
|
A:HIS397
|
3.1
|
6.6
|
1.0
|
CG
|
A:HIS397
|
3.1
|
6.3
|
1.0
|
HB2
|
A:HIS458
|
3.1
|
7.0
|
1.0
|
HE1
|
A:HIS458
|
3.2
|
7.2
|
1.0
|
HB3
|
A:HIS458
|
3.3
|
7.0
|
1.0
|
CB
|
A:CYS453
|
3.3
|
6.4
|
1.0
|
HB2
|
A:CYS453
|
3.4
|
6.5
|
1.0
|
CB
|
A:HIS458
|
3.4
|
7.0
|
1.0
|
HA
|
A:HIS397
|
3.4
|
6.6
|
1.0
|
HB3
|
A:CYS453
|
3.4
|
6.5
|
1.0
|
CB
|
A:HIS397
|
3.5
|
6.7
|
1.0
|
HE2
|
A:PHE463
|
3.5
|
6.6
|
1.0
|
CD1
|
A:ILE455
|
3.6
|
5.8
|
1.0
|
HD2
|
A:PRO398
|
3.8
|
6.1
|
1.0
|
CD2
|
A:PHE463
|
3.8
|
6.3
|
1.0
|
CB
|
A:ILE455
|
3.9
|
6.3
|
1.0
|
H
|
A:ILE455
|
3.9
|
7.0
|
1.0
|
HD12
|
A:ILE455
|
3.9
|
6.0
|
1.0
|
CA
|
A:HIS397
|
4.0
|
6.7
|
1.0
|
CG1
|
A:ILE455
|
4.1
|
6.3
|
1.0
|
HG13
|
A:ILE455
|
4.1
|
6.2
|
1.0
|
CE2
|
A:PHE463
|
4.1
|
6.8
|
1.0
|
NE2
|
A:HIS397
|
4.1
|
7.3
|
1.0
|
NE2
|
A:HIS458
|
4.1
|
7.4
|
1.0
|
CD2
|
A:HIS458
|
4.2
|
6.9
|
1.0
|
CD2
|
A:HIS397
|
4.2
|
7.1
|
1.0
|
HD13
|
A:ILE455
|
4.2
|
6.0
|
1.0
|
HB2
|
A:HIS397
|
4.4
|
6.6
|
1.0
|
HG21
|
A:ILE455
|
4.5
|
6.5
|
1.0
|
O
|
A:GLY394
|
4.6
|
9.2
|
1.0
|
HG22
|
A:ILE455
|
4.6
|
6.5
|
1.0
|
HZ
|
A:PHE341
|
4.6
|
7.8
|
1.0
|
CD
|
A:PRO398
|
4.6
|
6.0
|
1.0
|
CG2
|
A:ILE455
|
4.6
|
6.7
|
1.0
|
CA
|
A:CYS453
|
4.7
|
6.2
|
1.0
|
CZ
|
A:PHE341
|
4.8
|
7.9
|
1.0
|
N
|
A:ILE455
|
4.8
|
6.9
|
1.0
|
HD3
|
A:PRO398
|
4.8
|
6.1
|
1.0
|
HE2
|
A:PHE341
|
4.8
|
7.6
|
1.0
|
HE1
|
A:PHE399
|
4.9
|
7.9
|
1.0
|
HA
|
A:CYS453
|
4.9
|
6.2
|
1.0
|
HE2
|
A:HIS397
|
4.9
|
7.2
|
1.0
|
CA
|
A:HIS458
|
4.9
|
7.2
|
1.0
|
CE2
|
A:PHE341
|
4.9
|
7.3
|
1.0
|
CA
|
A:ILE455
|
4.9
|
6.8
|
1.0
|
HE2
|
A:HIS458
|
4.9
|
7.3
|
1.0
|
C
|
A:HIS397
|
5.0
|
6.3
|
1.0
|
N
|
A:HIS397
|
5.0
|
6.6
|
1.0
|
O
|
A:ILE455
|
5.0
|
7.0
|
1.0
|
HB3
|
A:PHE463
|
5.0
|
6.7
|
1.0
|
HG12
|
A:ILE455
|
5.0
|
6.2
|
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 04:36:15 2024
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