Copper in PDB 6ri8: Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
Enzymatic activity of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
All present enzymatic activity of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.:
1.10.3.2;
Protein crystallography data
The structure of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose., PDB code: 6ri8
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)
|
67.35 /
0.95
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.180,
84.200,
112.220,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
10.6 /
11.9
|
Other elements in 6ri8:
The structure of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose. also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
(pdb code 6ri8). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 7 binding sites of Copper where determined in the
Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose., PDB code: 6ri8:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
Copper binding site 1 out
of 7 in 6ri8
Go back to
Copper Binding Sites List in 6ri8
Copper binding site 1 out
of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:7.1
occ:0.65
|
CU
|
A:CU501
|
0.0
|
7.1
|
0.7
|
|
CU
|
A:CU501
|
0.7
|
6.9
|
0.3
|
|
NE2
|
A:HIS452
|
1.9
|
9.4
|
1.0
|
|
NE2
|
A:HIS402
|
2.0
|
6.6
|
1.0
|
|
NE2
|
A:HIS112
|
2.0
|
7.5
|
1.0
|
|
O
|
A:HOH602
|
2.4
|
8.6
|
0.4
|
|
O1
|
A:OXY511
|
2.4
|
9.2
|
0.2
|
|
O2
|
A:OXY511
|
2.5
|
8.3
|
0.2
|
|
CD2
|
A:HIS452
|
2.9
|
8.7
|
1.0
|
|
CE1
|
A:HIS402
|
2.9
|
6.6
|
1.0
|
|
O
|
A:HOH604
|
2.9
|
7.2
|
0.3
|
|
CE1
|
A:HIS112
|
2.9
|
7.8
|
1.0
|
|
CE1
|
A:HIS452
|
3.0
|
8.3
|
1.0
|
|
HE1
|
A:HIS402
|
3.0
|
7.7
|
1.0
|
|
CD2
|
A:HIS402
|
3.0
|
6.3
|
1.0
|
|
HD2
|
A:HIS452
|
3.0
|
9.2
|
1.0
|
|
HE1
|
A:HIS112
|
3.1
|
8.4
|
1.0
|
|
CD2
|
A:HIS112
|
3.1
|
6.9
|
1.0
|
|
HD2
|
A:PHE450
|
3.2
|
8.4
|
1.0
|
|
HE1
|
A:HIS452
|
3.2
|
9.2
|
1.0
|
|
HD2
|
A:HIS402
|
3.3
|
7.7
|
1.0
|
|
HD2
|
A:HIS112
|
3.3
|
8.4
|
1.0
|
|
HD2
|
A:HIS400
|
3.4
|
7.1
|
1.0
|
|
HB3
|
A:PHE450
|
3.6
|
7.7
|
1.0
|
|
O
|
A:HOH611
|
3.7
|
6.9
|
0.1
|
|
O
|
A:HOH615
|
3.8
|
13.2
|
0.8
|
|
CD2
|
A:PHE450
|
3.9
|
7.6
|
1.0
|
|
CG
|
A:HIS452
|
4.0
|
7.7
|
1.0
|
|
ND1
|
A:HIS452
|
4.0
|
7.8
|
1.0
|
|
ND1
|
A:HIS402
|
4.0
|
6.4
|
1.0
|
|
HB3
|
A:PRO80
|
4.1
|
7.6
|
1.0
|
|
ND1
|
A:HIS112
|
4.1
|
7.4
|
1.0
|
|
CG
|
A:HIS402
|
4.1
|
6.2
|
1.0
|
|
CD2
|
A:HIS400
|
4.2
|
6.7
|
1.0
|
|
CG
|
A:HIS112
|
4.2
|
6.5
|
1.0
|
|
HE1
|
A:HIS110
|
4.3
|
8.7
|
1.0
|
|
CU
|
A:CU503
|
4.3
|
6.7
|
0.4
|
|
CB
|
A:PHE450
|
4.3
|
7.0
|
1.0
|
|
CU
|
A:CU503
|
4.3
|
6.5
|
0.5
|
|
HD2
|
A:HIS65
|
4.4
|
7.4
|
1.0
|
|
HD21
|
A:LEU459
|
4.4
|
9.3
|
1.0
|
|
HB2
|
A:PHE450
|
4.4
|
7.7
|
1.0
|
|
CD2
|
A:HIS65
|
4.5
|
6.8
|
1.0
|
|
CG
|
A:PHE450
|
4.5
|
6.6
|
1.0
|
|
NE2
|
A:HIS65
|
4.5
|
6.6
|
1.0
|
|
HE2
|
A:PHE450
|
4.6
|
8.4
|
1.0
|
|
CE2
|
A:PHE450
|
4.7
|
9.1
|
1.0
|
|
CU
|
A:CU502
|
4.7
|
9.7
|
0.3
|
|
NE2
|
A:HIS400
|
4.7
|
6.8
|
1.0
|
|
HD1
|
A:HIS402
|
4.8
|
7.7
|
1.0
|
|
HD1
|
A:HIS452
|
4.8
|
9.2
|
1.0
|
|
HD1
|
A:HIS112
|
4.9
|
8.4
|
1.0
|
|
HD22
|
A:LEU459
|
4.9
|
9.3
|
1.0
|
|
HD2
|
A:HIS454
|
5.0
|
6.3
|
1.0
|
|
CB
|
A:PRO80
|
5.0
|
7.0
|
1.0
|
|
Copper binding site 2 out
of 7 in 6ri8
Go back to
Copper Binding Sites List in 6ri8
Copper binding site 2 out
of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:6.9
occ:0.30
|
CU
|
A:CU501
|
0.0
|
6.9
|
0.3
|
|
CU
|
A:CU501
|
0.7
|
7.1
|
0.7
|
|
O
|
A:HOH602
|
1.7
|
8.6
|
0.4
|
|
O2
|
A:OXY511
|
1.8
|
8.3
|
0.2
|
|
O1
|
A:OXY511
|
1.9
|
9.2
|
0.2
|
|
NE2
|
A:HIS402
|
2.0
|
6.6
|
1.0
|
|
NE2
|
A:HIS112
|
2.2
|
7.5
|
1.0
|
|
O
|
A:HOH604
|
2.2
|
7.2
|
0.3
|
|
NE2
|
A:HIS452
|
2.2
|
9.4
|
1.0
|
|
CE1
|
A:HIS402
|
3.0
|
6.6
|
1.0
|
|
O
|
A:HOH611
|
3.0
|
6.9
|
0.1
|
|
CD2
|
A:HIS112
|
3.0
|
6.9
|
1.0
|
|
HD2
|
A:HIS400
|
3.0
|
7.1
|
1.0
|
|
HD2
|
A:HIS112
|
3.1
|
8.4
|
1.0
|
|
CE1
|
A:HIS452
|
3.1
|
8.3
|
1.0
|
|
HE1
|
A:HIS402
|
3.1
|
7.7
|
1.0
|
|
CD2
|
A:HIS402
|
3.1
|
6.3
|
1.0
|
|
HE1
|
A:HIS452
|
3.1
|
9.2
|
1.0
|
|
CE1
|
A:HIS112
|
3.3
|
7.8
|
1.0
|
|
HD2
|
A:HIS402
|
3.4
|
7.7
|
1.0
|
|
CD2
|
A:HIS452
|
3.4
|
8.7
|
1.0
|
|
HE1
|
A:HIS112
|
3.5
|
8.4
|
1.0
|
|
O
|
A:HOH615
|
3.6
|
13.2
|
0.8
|
|
HD2
|
A:HIS452
|
3.6
|
9.2
|
1.0
|
|
HD2
|
A:HIS65
|
3.7
|
7.4
|
1.0
|
|
HE1
|
A:HIS110
|
3.8
|
8.7
|
1.0
|
|
CU
|
A:CU503
|
3.8
|
6.7
|
0.4
|
|
CD2
|
A:HIS400
|
3.8
|
6.7
|
1.0
|
|
CU
|
A:CU503
|
3.8
|
6.5
|
0.5
|
|
HD2
|
A:PHE450
|
3.9
|
8.4
|
1.0
|
|
CD2
|
A:HIS65
|
3.9
|
6.8
|
1.0
|
|
CU
|
A:CU502
|
4.0
|
9.7
|
0.3
|
|
NE2
|
A:HIS65
|
4.0
|
6.6
|
1.0
|
|
ND1
|
A:HIS402
|
4.1
|
6.4
|
1.0
|
|
HB3
|
A:PHE450
|
4.1
|
7.7
|
1.0
|
|
CG
|
A:HIS402
|
4.2
|
6.2
|
1.0
|
|
CG
|
A:HIS112
|
4.2
|
6.5
|
1.0
|
|
NE2
|
A:HIS400
|
4.3
|
6.8
|
1.0
|
|
ND1
|
A:HIS452
|
4.3
|
7.8
|
1.0
|
|
ND1
|
A:HIS112
|
4.3
|
7.4
|
1.0
|
|
HB3
|
A:PRO80
|
4.4
|
7.6
|
1.0
|
|
CG
|
A:HIS452
|
4.4
|
7.7
|
1.0
|
|
HD2
|
A:HIS454
|
4.5
|
6.3
|
1.0
|
|
NE2
|
A:HIS454
|
4.5
|
6.6
|
1.0
|
|
CU
|
A:CU502
|
4.5
|
5.3
|
0.7
|
|
CE1
|
A:HIS110
|
4.6
|
6.7
|
1.0
|
|
CD2
|
A:PHE450
|
4.6
|
7.6
|
1.0
|
|
CG
|
A:HIS65
|
4.7
|
6.5
|
1.0
|
|
CD2
|
A:HIS454
|
4.7
|
6.2
|
1.0
|
|
HD21
|
A:LEU459
|
4.7
|
9.3
|
1.0
|
|
CE1
|
A:HIS65
|
4.8
|
6.5
|
1.0
|
|
HD1
|
A:HIS402
|
4.9
|
7.7
|
1.0
|
|
NE2
|
A:HIS110
|
4.9
|
6.6
|
1.0
|
|
CB
|
A:PHE450
|
5.0
|
7.0
|
1.0
|
|
Copper binding site 3 out
of 7 in 6ri8
Go back to
Copper Binding Sites List in 6ri8
Copper binding site 3 out
of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:5.3
occ:0.65
|
CU
|
A:CU502
|
0.0
|
5.3
|
0.7
|
|
CU
|
A:CU502
|
0.6
|
9.7
|
0.3
|
|
ND1
|
A:HIS67
|
1.9
|
6.2
|
1.0
|
|
NE2
|
A:HIS110
|
2.0
|
6.6
|
1.0
|
|
NE2
|
A:HIS454
|
2.1
|
6.6
|
1.0
|
|
O
|
A:HOH611
|
2.3
|
6.9
|
0.1
|
|
O2
|
A:OXY511
|
2.7
|
8.3
|
0.2
|
|
HB2
|
A:HIS67
|
2.8
|
6.3
|
1.0
|
|
O
|
A:HOH604
|
2.8
|
7.2
|
0.3
|
|
CE1
|
A:HIS67
|
2.9
|
6.0
|
1.0
|
|
CG
|
A:HIS67
|
2.9
|
6.3
|
1.0
|
|
CD2
|
A:HIS110
|
3.0
|
6.5
|
1.0
|
|
CE1
|
A:HIS110
|
3.0
|
6.7
|
1.0
|
|
CE1
|
A:HIS454
|
3.0
|
6.5
|
1.0
|
|
O
|
A:HOH602
|
3.0
|
8.6
|
0.4
|
|
HD2
|
A:HIS65
|
3.1
|
7.4
|
1.0
|
|
HE1
|
A:HIS67
|
3.1
|
6.3
|
1.0
|
|
HE1
|
A:HIS454
|
3.1
|
6.3
|
1.0
|
|
HD2
|
A:HIS110
|
3.1
|
8.7
|
1.0
|
|
CD2
|
A:HIS454
|
3.2
|
6.2
|
1.0
|
|
HE1
|
A:HIS110
|
3.2
|
8.7
|
1.0
|
|
CB
|
A:HIS67
|
3.4
|
6.2
|
1.0
|
|
O1
|
A:OXY511
|
3.4
|
9.2
|
0.2
|
|
HZ2
|
A:TRP108
|
3.4
|
8.2
|
1.0
|
|
HD2
|
A:HIS454
|
3.4
|
6.3
|
1.0
|
|
HB2
|
A:ALA244
|
3.6
|
8.2
|
1.0
|
|
CZ2
|
A:TRP108
|
3.7
|
6.8
|
1.0
|
|
CD2
|
A:HIS65
|
3.9
|
6.8
|
1.0
|
|
HE1
|
A:TRP108
|
3.9
|
8.2
|
1.0
|
|
CE2
|
A:TRP108
|
3.9
|
6.3
|
1.0
|
|
CU
|
A:CU503
|
4.0
|
6.7
|
0.4
|
|
HB3
|
A:HIS67
|
4.0
|
6.3
|
1.0
|
|
CU
|
A:CU503
|
4.0
|
6.5
|
0.5
|
|
NE2
|
A:HIS67
|
4.0
|
6.5
|
1.0
|
|
CD2
|
A:HIS67
|
4.1
|
6.6
|
1.0
|
|
NE1
|
A:TRP108
|
4.1
|
6.5
|
1.0
|
|
ND1
|
A:HIS110
|
4.1
|
6.5
|
1.0
|
|
CG
|
A:HIS110
|
4.1
|
6.3
|
1.0
|
|
ND1
|
A:HIS454
|
4.2
|
6.2
|
1.0
|
|
HA
|
A:HIS67
|
4.2
|
6.1
|
1.0
|
|
HD2
|
A:HIS400
|
4.3
|
7.1
|
1.0
|
|
CG
|
A:HIS454
|
4.3
|
6.0
|
1.0
|
|
NE2
|
A:HIS65
|
4.3
|
6.6
|
1.0
|
|
HB1
|
A:ALA244
|
4.3
|
8.2
|
1.0
|
|
CB
|
A:ALA244
|
4.4
|
6.3
|
1.0
|
|
NE2
|
A:HIS400
|
4.4
|
6.8
|
1.0
|
|
CD2
|
A:HIS400
|
4.4
|
6.7
|
1.0
|
|
CA
|
A:HIS67
|
4.4
|
5.9
|
1.0
|
|
CH2
|
A:TRP108
|
4.5
|
6.9
|
1.0
|
|
O
|
A:HOH615
|
4.5
|
13.2
|
0.8
|
|
CU
|
A:CU501
|
4.5
|
6.9
|
0.3
|
|
HH2
|
A:TRP108
|
4.7
|
8.2
|
1.0
|
|
HB3
|
A:ALA244
|
4.8
|
8.2
|
1.0
|
|
HE2
|
A:HIS67
|
4.8
|
6.3
|
1.0
|
|
CD2
|
A:TRP108
|
4.9
|
6.3
|
1.0
|
|
HD1
|
A:HIS110
|
4.9
|
8.7
|
1.0
|
|
HD1
|
A:HIS454
|
4.9
|
6.3
|
1.0
|
|
HD2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
|
HD2
|
A:HIS112
|
5.0
|
8.4
|
1.0
|
|
CD1
|
A:TRP108
|
5.0
|
6.4
|
1.0
|
|
HE1
|
A:HIS452
|
5.0
|
9.2
|
1.0
|
|
Copper binding site 4 out
of 7 in 6ri8
Go back to
Copper Binding Sites List in 6ri8
Copper binding site 4 out
of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:9.7
occ:0.30
|
CU
|
A:CU502
|
0.0
|
9.7
|
0.3
|
|
CU
|
A:CU502
|
0.6
|
5.3
|
0.7
|
|
O
|
A:HOH611
|
1.9
|
6.9
|
0.1
|
|
NE2
|
A:HIS454
|
2.0
|
6.6
|
1.0
|
|
NE2
|
A:HIS110
|
2.1
|
6.6
|
1.0
|
|
O2
|
A:OXY511
|
2.2
|
8.3
|
0.2
|
|
ND1
|
A:HIS67
|
2.2
|
6.2
|
1.0
|
|
O
|
A:HOH604
|
2.3
|
7.2
|
0.3
|
|
O
|
A:HOH602
|
2.5
|
8.6
|
0.4
|
|
O1
|
A:OXY511
|
2.8
|
9.2
|
0.2
|
|
CE1
|
A:HIS110
|
2.9
|
6.7
|
1.0
|
|
HD2
|
A:HIS65
|
2.9
|
7.4
|
1.0
|
|
HE1
|
A:HIS110
|
3.0
|
8.7
|
1.0
|
|
CE1
|
A:HIS454
|
3.0
|
6.5
|
1.0
|
|
CD2
|
A:HIS454
|
3.0
|
6.2
|
1.0
|
|
CE1
|
A:HIS67
|
3.1
|
6.0
|
1.0
|
|
HB2
|
A:HIS67
|
3.1
|
6.3
|
1.0
|
|
HE1
|
A:HIS454
|
3.1
|
6.3
|
1.0
|
|
HE1
|
A:HIS67
|
3.2
|
6.3
|
1.0
|
|
HD2
|
A:HIS454
|
3.2
|
6.3
|
1.0
|
|
CD2
|
A:HIS110
|
3.2
|
6.5
|
1.0
|
|
CG
|
A:HIS67
|
3.3
|
6.3
|
1.0
|
|
HD2
|
A:HIS110
|
3.5
|
8.7
|
1.0
|
|
CD2
|
A:HIS65
|
3.7
|
6.8
|
1.0
|
|
CU
|
A:CU503
|
3.7
|
6.7
|
0.4
|
|
CB
|
A:HIS67
|
3.7
|
6.2
|
1.0
|
|
CU
|
A:CU503
|
3.8
|
6.5
|
0.5
|
|
HD2
|
A:HIS400
|
3.8
|
7.1
|
1.0
|
|
HZ2
|
A:TRP108
|
3.9
|
8.2
|
1.0
|
|
HB2
|
A:ALA244
|
3.9
|
8.2
|
1.0
|
|
CU
|
A:CU501
|
4.0
|
6.9
|
0.3
|
|
CD2
|
A:HIS400
|
4.0
|
6.7
|
1.0
|
|
O
|
A:HOH615
|
4.1
|
13.2
|
0.8
|
|
NE2
|
A:HIS65
|
4.1
|
6.6
|
1.0
|
|
ND1
|
A:HIS110
|
4.1
|
6.5
|
1.0
|
|
ND1
|
A:HIS454
|
4.1
|
6.2
|
1.0
|
|
NE2
|
A:HIS400
|
4.1
|
6.8
|
1.0
|
|
CG
|
A:HIS454
|
4.1
|
6.0
|
1.0
|
|
CZ2
|
A:TRP108
|
4.2
|
6.8
|
1.0
|
|
NE2
|
A:HIS67
|
4.3
|
6.5
|
1.0
|
|
CG
|
A:HIS110
|
4.3
|
6.3
|
1.0
|
|
HA
|
A:HIS67
|
4.3
|
6.1
|
1.0
|
|
CD2
|
A:HIS67
|
4.4
|
6.6
|
1.0
|
|
HB3
|
A:HIS67
|
4.4
|
6.3
|
1.0
|
|
HE1
|
A:TRP108
|
4.4
|
8.2
|
1.0
|
|
CE2
|
A:TRP108
|
4.5
|
6.3
|
1.0
|
|
HE1
|
A:HIS452
|
4.5
|
9.2
|
1.0
|
|
HB1
|
A:ALA244
|
4.5
|
8.2
|
1.0
|
|
HD2
|
A:HIS112
|
4.6
|
8.4
|
1.0
|
|
CB
|
A:ALA244
|
4.6
|
6.3
|
1.0
|
|
NE1
|
A:TRP108
|
4.6
|
6.5
|
1.0
|
|
CA
|
A:HIS67
|
4.7
|
5.9
|
1.0
|
|
CU
|
A:CU501
|
4.7
|
7.1
|
0.7
|
|
HD1
|
A:HIS110
|
4.8
|
8.7
|
1.0
|
|
HD1
|
A:HIS454
|
4.9
|
6.3
|
1.0
|
|
CH2
|
A:TRP108
|
4.9
|
6.9
|
1.0
|
|
CG
|
A:HIS65
|
4.9
|
6.5
|
1.0
|
|
CG
|
A:HIS400
|
4.9
|
6.5
|
1.0
|
|
HB3
|
A:ALA244
|
5.0
|
8.2
|
1.0
|
|
CE1
|
A:HIS400
|
5.0
|
6.6
|
1.0
|
|
Copper binding site 5 out
of 7 in 6ri8
Go back to
Copper Binding Sites List in 6ri8
Copper binding site 5 out
of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:6.7
occ:0.38
|
CU
|
A:CU503
|
0.0
|
6.7
|
0.4
|
|
CU
|
A:CU503
|
0.1
|
6.5
|
0.5
|
|
F
|
A:F509
|
1.8
|
8.7
|
0.5
|
|
O
|
A:HOH611
|
1.9
|
6.9
|
0.1
|
|
NE2
|
A:HIS400
|
1.9
|
6.8
|
1.0
|
|
NE2
|
A:HIS65
|
1.9
|
6.6
|
1.0
|
|
O
|
A:HOH604
|
2.1
|
7.2
|
0.3
|
|
O
|
A:HOH743
|
2.6
|
7.5
|
0.2
|
|
F
|
A:F509
|
2.6
|
11.0
|
0.4
|
|
CE1
|
A:HIS65
|
2.9
|
6.5
|
1.0
|
|
CD2
|
A:HIS400
|
2.9
|
6.7
|
1.0
|
|
CE1
|
A:HIS400
|
2.9
|
6.6
|
1.0
|
|
CD2
|
A:HIS65
|
2.9
|
6.8
|
1.0
|
|
HA
|
A:HIS67
|
3.0
|
6.1
|
1.0
|
|
HE1
|
A:HIS65
|
3.0
|
7.4
|
1.0
|
|
HD2
|
A:HIS400
|
3.1
|
7.1
|
1.0
|
|
HE1
|
A:HIS400
|
3.1
|
7.1
|
1.0
|
|
HD2
|
A:HIS65
|
3.2
|
7.4
|
1.0
|
|
H
|
A:GLY68
|
3.2
|
6.1
|
1.0
|
|
O2
|
A:OXY511
|
3.3
|
8.3
|
0.2
|
|
CD2
|
A:HIS402
|
3.3
|
6.3
|
1.0
|
|
NE2
|
A:HIS402
|
3.4
|
6.6
|
1.0
|
|
HD2
|
A:HIS402
|
3.5
|
7.7
|
1.0
|
|
ND1
|
A:HIS67
|
3.5
|
6.2
|
1.0
|
|
CU
|
A:CU502
|
3.7
|
9.7
|
0.3
|
|
HA
|
A:HIS402
|
3.7
|
7.5
|
1.0
|
|
CG
|
A:HIS402
|
3.7
|
6.2
|
1.0
|
|
CG
|
A:HIS67
|
3.8
|
6.3
|
1.0
|
|
CE1
|
A:HIS402
|
3.8
|
6.6
|
1.0
|
|
CU
|
A:CU501
|
3.8
|
6.9
|
0.3
|
|
O
|
A:HOH602
|
3.8
|
8.6
|
0.4
|
|
CE1
|
A:HIS67
|
3.9
|
6.0
|
1.0
|
|
CA
|
A:HIS67
|
3.9
|
5.9
|
1.0
|
|
CU
|
A:CU502
|
4.0
|
5.3
|
0.7
|
|
ND1
|
A:HIS402
|
4.0
|
6.4
|
1.0
|
|
ND1
|
A:HIS65
|
4.0
|
6.6
|
1.0
|
|
ND1
|
A:HIS400
|
4.0
|
6.5
|
1.0
|
|
N
|
A:GLY68
|
4.0
|
6.1
|
1.0
|
|
CG
|
A:HIS400
|
4.0
|
6.5
|
1.0
|
|
CG
|
A:HIS65
|
4.1
|
6.5
|
1.0
|
|
HB2
|
A:HIS67
|
4.2
|
6.3
|
1.0
|
|
HE1
|
A:HIS67
|
4.2
|
6.3
|
1.0
|
|
CB
|
A:HIS67
|
4.2
|
6.2
|
1.0
|
|
HE1
|
A:HIS402
|
4.3
|
7.7
|
1.0
|
|
CU
|
A:CU501
|
4.3
|
7.1
|
0.7
|
|
CD2
|
A:HIS67
|
4.3
|
6.6
|
1.0
|
|
NE2
|
A:HIS67
|
4.4
|
6.5
|
1.0
|
|
CA
|
A:HIS402
|
4.5
|
6.3
|
1.0
|
|
O1
|
A:OXY511
|
4.5
|
9.2
|
0.2
|
|
C
|
A:HIS67
|
4.5
|
5.9
|
1.0
|
|
HD1
|
A:HIS402
|
4.5
|
7.7
|
1.0
|
|
CB
|
A:HIS402
|
4.6
|
6.6
|
1.0
|
|
O
|
A:HOH870
|
4.6
|
11.4
|
1.0
|
|
O
|
A:HOH930
|
4.7
|
10.3
|
1.0
|
|
HD1
|
A:HIS65
|
4.8
|
7.4
|
1.0
|
|
HD1
|
A:HIS400
|
4.8
|
7.1
|
1.0
|
|
HB3
|
A:HIS402
|
4.8
|
7.7
|
1.0
|
|
N
|
A:HIS402
|
4.8
|
6.1
|
1.0
|
|
HA2
|
A:GLY68
|
4.9
|
7.2
|
1.0
|
|
HD2
|
A:HIS454
|
4.9
|
6.3
|
1.0
|
|
HD2
|
A:HIS112
|
4.9
|
8.4
|
1.0
|
|
HD2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
|
N
|
A:HIS67
|
4.9
|
5.8
|
1.0
|
|
HE2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
|
O
|
A:LEU401
|
5.0
|
6.8
|
1.0
|
|
Copper binding site 6 out
of 7 in 6ri8
Go back to
Copper Binding Sites List in 6ri8
Copper binding site 6 out
of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu503
b:6.5
occ:0.45
|
CU
|
A:CU503
|
0.0
|
6.5
|
0.5
|
|
CU
|
A:CU503
|
0.1
|
6.7
|
0.4
|
|
F
|
A:F509
|
1.8
|
8.7
|
0.5
|
|
NE2
|
A:HIS400
|
1.9
|
6.8
|
1.0
|
|
NE2
|
A:HIS65
|
1.9
|
6.6
|
1.0
|
|
O
|
A:HOH611
|
1.9
|
6.9
|
0.1
|
|
O
|
A:HOH604
|
2.1
|
7.2
|
0.3
|
|
O
|
A:HOH743
|
2.5
|
7.5
|
0.2
|
|
F
|
A:F509
|
2.6
|
11.0
|
0.4
|
|
CE1
|
A:HIS65
|
2.8
|
6.5
|
1.0
|
|
CE1
|
A:HIS400
|
2.9
|
6.6
|
1.0
|
|
CD2
|
A:HIS400
|
2.9
|
6.7
|
1.0
|
|
CD2
|
A:HIS65
|
2.9
|
6.8
|
1.0
|
|
HA
|
A:HIS67
|
3.0
|
6.1
|
1.0
|
|
HE1
|
A:HIS65
|
3.0
|
7.4
|
1.0
|
|
HE1
|
A:HIS400
|
3.1
|
7.1
|
1.0
|
|
HD2
|
A:HIS400
|
3.1
|
7.1
|
1.0
|
|
H
|
A:GLY68
|
3.2
|
6.1
|
1.0
|
|
HD2
|
A:HIS65
|
3.2
|
7.4
|
1.0
|
|
CD2
|
A:HIS402
|
3.3
|
6.3
|
1.0
|
|
O2
|
A:OXY511
|
3.3
|
8.3
|
0.2
|
|
NE2
|
A:HIS402
|
3.4
|
6.6
|
1.0
|
|
HD2
|
A:HIS402
|
3.5
|
7.7
|
1.0
|
|
ND1
|
A:HIS67
|
3.5
|
6.2
|
1.0
|
|
HA
|
A:HIS402
|
3.7
|
7.5
|
1.0
|
|
CG
|
A:HIS402
|
3.7
|
6.2
|
1.0
|
|
CU
|
A:CU502
|
3.8
|
9.7
|
0.3
|
|
CE1
|
A:HIS402
|
3.8
|
6.6
|
1.0
|
|
CG
|
A:HIS67
|
3.8
|
6.3
|
1.0
|
|
CU
|
A:CU501
|
3.8
|
6.9
|
0.3
|
|
O
|
A:HOH602
|
3.9
|
8.6
|
0.4
|
|
CA
|
A:HIS67
|
3.9
|
5.9
|
1.0
|
|
CE1
|
A:HIS67
|
3.9
|
6.0
|
1.0
|
|
ND1
|
A:HIS402
|
4.0
|
6.4
|
1.0
|
|
ND1
|
A:HIS65
|
4.0
|
6.6
|
1.0
|
|
N
|
A:GLY68
|
4.0
|
6.1
|
1.0
|
|
ND1
|
A:HIS400
|
4.0
|
6.5
|
1.0
|
|
CU
|
A:CU502
|
4.0
|
5.3
|
0.7
|
|
CG
|
A:HIS400
|
4.0
|
6.5
|
1.0
|
|
CG
|
A:HIS65
|
4.1
|
6.5
|
1.0
|
|
HB2
|
A:HIS67
|
4.2
|
6.3
|
1.0
|
|
CB
|
A:HIS67
|
4.2
|
6.2
|
1.0
|
|
HE1
|
A:HIS67
|
4.2
|
6.3
|
1.0
|
|
HE1
|
A:HIS402
|
4.3
|
7.7
|
1.0
|
|
CU
|
A:CU501
|
4.3
|
7.1
|
0.7
|
|
CD2
|
A:HIS67
|
4.3
|
6.6
|
1.0
|
|
NE2
|
A:HIS67
|
4.4
|
6.5
|
1.0
|
|
CA
|
A:HIS402
|
4.4
|
6.3
|
1.0
|
|
C
|
A:HIS67
|
4.5
|
5.9
|
1.0
|
|
O1
|
A:OXY511
|
4.5
|
9.2
|
0.2
|
|
HD1
|
A:HIS402
|
4.5
|
7.7
|
1.0
|
|
CB
|
A:HIS402
|
4.5
|
6.6
|
1.0
|
|
O
|
A:HOH870
|
4.5
|
11.4
|
1.0
|
|
O
|
A:HOH930
|
4.7
|
10.3
|
1.0
|
|
HB3
|
A:HIS402
|
4.7
|
7.7
|
1.0
|
|
HD1
|
A:HIS65
|
4.7
|
7.4
|
1.0
|
|
N
|
A:HIS402
|
4.8
|
6.1
|
1.0
|
|
HD1
|
A:HIS400
|
4.8
|
7.1
|
1.0
|
|
HA2
|
A:GLY68
|
4.8
|
7.2
|
1.0
|
|
HD2
|
A:HIS454
|
4.9
|
6.3
|
1.0
|
|
HD2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
|
HD2
|
A:HIS112
|
4.9
|
8.4
|
1.0
|
|
N
|
A:HIS67
|
4.9
|
5.8
|
1.0
|
|
HE2
|
A:HIS67
|
4.9
|
6.3
|
1.0
|
|
O
|
A:LEU401
|
5.0
|
6.8
|
1.0
|
|
Copper binding site 7 out
of 7 in 6ri8
Go back to
Copper Binding Sites List in 6ri8
Copper binding site 7 out
of 7 in the Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose.
 Mono view
 Stereo pair view
|
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Single Crystal Serial Study of the Inhibition of Laccases From Steccherinum Murashkinskyi By Fluoride Anions at Sub-Atomic Resolution. Third Structure of the Series with 800 Kgy Dose. within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu504
b:6.4
occ:0.85
|
ND1
|
A:HIS458
|
2.0
|
7.1
|
1.0
|
|
ND1
|
A:HIS397
|
2.0
|
7.1
|
1.0
|
|
SG
|
A:CYS453
|
2.2
|
7.2
|
1.0
|
|
HD11
|
A:ILE455
|
2.6
|
8.0
|
1.0
|
|
HB
|
A:ILE455
|
2.9
|
8.0
|
1.0
|
|
CE1
|
A:HIS397
|
2.9
|
7.5
|
1.0
|
|
CE1
|
A:HIS458
|
3.0
|
7.5
|
1.0
|
|
CG
|
A:HIS458
|
3.0
|
7.0
|
1.0
|
|
HD2
|
A:PHE463
|
3.1
|
11.0
|
1.0
|
|
HB3
|
A:HIS397
|
3.1
|
10.8
|
1.0
|
|
HE1
|
A:HIS397
|
3.1
|
7.8
|
1.0
|
|
CG
|
A:HIS397
|
3.1
|
7.2
|
1.0
|
|
HB2
|
A:HIS458
|
3.1
|
8.0
|
1.0
|
|
HE1
|
A:HIS458
|
3.2
|
7.8
|
1.0
|
|
HB3
|
A:HIS458
|
3.3
|
8.0
|
1.0
|
|
CB
|
A:CYS453
|
3.3
|
7.0
|
1.0
|
|
CB
|
A:HIS458
|
3.4
|
7.1
|
1.0
|
|
HA
|
A:HIS397
|
3.4
|
8.0
|
1.0
|
|
HB2
|
A:CYS453
|
3.4
|
7.0
|
1.0
|
|
HB3
|
A:CYS453
|
3.4
|
7.0
|
1.0
|
|
CB
|
A:HIS397
|
3.5
|
7.2
|
1.0
|
|
HE2
|
A:PHE463
|
3.5
|
11.0
|
1.0
|
|
CD1
|
A:ILE455
|
3.6
|
7.6
|
1.0
|
|
HD2
|
A:PRO398
|
3.8
|
8.0
|
1.0
|
|
CB
|
A:ILE455
|
3.8
|
6.9
|
1.0
|
|
CD2
|
A:PHE463
|
3.8
|
7.1
|
1.0
|
|
H
|
A:ILE455
|
3.9
|
8.0
|
1.0
|
|
HD12
|
A:ILE455
|
4.0
|
8.0
|
1.0
|
|
CA
|
A:HIS397
|
4.0
|
6.9
|
1.0
|
|
CE2
|
A:PHE463
|
4.0
|
7.5
|
1.0
|
|
CG1
|
A:ILE455
|
4.0
|
7.3
|
1.0
|
|
NE2
|
A:HIS397
|
4.1
|
7.9
|
1.0
|
|
HG13
|
A:ILE455
|
4.1
|
8.0
|
1.0
|
|
NE2
|
A:HIS458
|
4.1
|
8.0
|
1.0
|
|
HD13
|
A:ILE455
|
4.2
|
8.0
|
1.0
|
|
CD2
|
A:HIS458
|
4.2
|
7.6
|
1.0
|
|
CD2
|
A:HIS397
|
4.2
|
8.0
|
1.0
|
|
HB2
|
A:HIS397
|
4.4
|
10.8
|
1.0
|
|
HG21
|
A:ILE455
|
4.5
|
8.0
|
1.0
|
|
HG22
|
A:ILE455
|
4.6
|
8.0
|
1.0
|
|
CG2
|
A:ILE455
|
4.6
|
7.2
|
1.0
|
|
HZ
|
A:PHE341
|
4.6
|
10.5
|
1.0
|
|
CD
|
A:PRO398
|
4.6
|
6.9
|
1.0
|
|
CA
|
A:CYS453
|
4.7
|
6.3
|
1.0
|
|
O
|
A:GLY394
|
4.7
|
10.6
|
1.0
|
|
N
|
A:ILE455
|
4.7
|
6.7
|
1.0
|
|
CZ
|
A:PHE341
|
4.8
|
9.2
|
1.0
|
|
HA2
|
A:GLY395
|
4.8
|
9.6
|
1.0
|
|
CA
|
A:ILE455
|
4.8
|
6.9
|
1.0
|
|
HE2
|
A:PHE341
|
4.8
|
10.5
|
1.0
|
|
HD3
|
A:PRO398
|
4.8
|
8.0
|
1.0
|
|
HA
|
A:CYS453
|
4.8
|
6.4
|
1.0
|
|
HE1
|
A:PHE399
|
4.8
|
10.8
|
1.0
|
|
HE2
|
A:HIS397
|
4.9
|
7.8
|
1.0
|
|
CE2
|
A:PHE341
|
4.9
|
8.6
|
1.0
|
|
CA
|
A:HIS458
|
4.9
|
7.2
|
1.0
|
|
HE2
|
A:HIS458
|
4.9
|
7.8
|
1.0
|
|
O
|
A:ILE455
|
4.9
|
7.3
|
1.0
|
|
C
|
A:HIS397
|
5.0
|
6.5
|
1.0
|
|
N
|
A:HIS397
|
5.0
|
7.4
|
1.0
|
|
HG12
|
A:ILE455
|
5.0
|
8.0
|
1.0
|
|
HB3
|
A:PHE463
|
5.0
|
8.0
|
1.0
|
|
Reference:
K.M.Polyakov,
S.Gavryushov,
T.V.Fedorova,
O.A.Glazunova,
A.N.Popov.
The Subatomic Resolution Study of Laccase Inhibition By Chloride and Fluoride Anions Using Single-Crystal Serial Crystallography: Insights Into the Enzymatic Reaction Mechanism. Acta Crystallogr D Struct V. 75 804 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31478903
DOI: 10.1107/S2059798319010684
Page generated: Wed Jul 31 07:21:48 2024
|
