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Copper in PDB 6rhp: Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).

Enzymatic activity of Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).

All present enzymatic activity of Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).:
1.10.3.2;

Protein crystallography data

The structure of Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing)., PDB code: 6rhp 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) 67.40 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.340, 84.250, 112.340, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 21.5

Copper Binding Sites:

The binding sites of Copper atom in the Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing). (pdb code 6rhp). 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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing)., PDB code: 6rhp:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7;

Copper binding site 1 out of 7 in 6rhp

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Copper binding site 1 out of 7 in the Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).


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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:14.4
occ:0.65
 CU A:CU501 0.0 14.4 0.7
CU A:CU501 0.8 5.7 0.3
NE2 A:HIS402 1.9 8.8 1.0
NE2 A:HIS452 1.9 11.9 1.0
NE2 A:HIS112 2.0 9.5 1.0
O A:HOH601 2.2 10.5 0.3
O1 A:OXY509 2.3 2.5 0.2
O2 A:OXY509 2.8 2.5 0.2
CD2 A:HIS452 2.8 12.2 1.0
CE1 A:HIS402 2.9 11.6 1.0
CE1 A:HIS112 2.9 10.6 1.0
HD2 A:HIS452 2.9 11.9 1.0
CD2 A:HIS402 2.9 9.3 1.0
CE1 A:HIS452 3.0 11.0 1.0
HE1 A:HIS112 3.0 10.6 1.0
CD2 A:HIS112 3.1 10.1 1.0
HE1 A:HIS402 3.1 10.4 1.0
HD2 A:HIS402 3.1 9.5 1.0
O A:HOH603 3.2 2.3 0.3
HD2 A:PHE450 3.3 12.1 1.0
HD2 A:HIS400 3.3 11.1 1.0
HE1 A:HIS452 3.3 11.4 1.0
HD2 A:HIS112 3.3 10.1 1.0
HB3 A:PHE450 3.7 10.7 1.0
O A:HOH605 3.9 19.2 1.0
CD2 A:PHE450 3.9 12.2 1.0
CG A:HIS452 4.0 11.4 1.0
ND1 A:HIS402 4.0 9.8 1.0
HB3 A:PRO80 4.0 10.9 1.0
ND1 A:HIS452 4.0 12.0 1.0
ND1 A:HIS112 4.1 11.8 1.0
CG A:HIS402 4.1 10.3 1.0
CD2 A:HIS400 4.2 10.4 1.0
CG A:HIS112 4.2 10.5 1.0
HE1 A:HIS110 4.3 8.8 1.0
CU A:CU502 4.3 9.2 0.3
HD2 A:HIS65 4.3 10.2 1.0
CU A:CU503 4.4 10.8 0.5
CU A:CU503 4.4 11.1 0.3
CD2 A:HIS65 4.5 11.3 1.0
CB A:PHE450 4.5 10.6 1.0
NE2 A:HIS65 4.5 9.6 1.0
HD21 A:LEU459 4.6 13.2 1.0
CG A:PHE450 4.6 11.7 1.0
HE2 A:PHE450 4.6 12.2 1.0
HB2 A:PHE450 4.7 10.7 1.0
CE2 A:PHE450 4.7 12.5 1.0
NE2 A:HIS400 4.8 13.1 1.0
HD1 A:HIS402 4.8 10.3 1.0
HD1 A:HIS112 4.8 11.2 1.0
HD1 A:HIS452 4.8 11.6 1.0
HD22 A:LEU459 4.9 13.2 1.0
CB A:PRO80 5.0 11.0 1.0

Copper binding site 2 out of 7 in 6rhp

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Copper binding site 2 out of 7 in the Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).


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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:5.7
occ:0.30
 CU A:CU501 0.0 5.7 0.3
CU A:CU501 0.8 14.4 0.7
O A:HOH601 1.5 10.5 0.3
O1 A:OXY509 1.5 2.5 0.2
NE2 A:HIS402 2.1 8.8 1.0
O2 A:OXY509 2.1 2.5 0.2
NE2 A:HIS112 2.2 9.5 1.0
NE2 A:HIS452 2.3 11.9 1.0
O A:HOH603 2.4 2.3 0.3
HD2 A:HIS400 2.9 11.1 1.0
CD2 A:HIS112 3.0 10.1 1.0
CE1 A:HIS402 3.0 11.6 1.0
HD2 A:HIS112 3.0 10.1 1.0
CD2 A:HIS402 3.1 9.3 1.0
CE1 A:HIS452 3.1 11.0 1.0
HE1 A:HIS452 3.2 11.4 1.0
HE1 A:HIS402 3.2 10.4 1.0
HD2 A:HIS402 3.3 9.5 1.0
CE1 A:HIS112 3.3 10.6 1.0
CD2 A:HIS452 3.3 12.2 1.0
CU A:CU502 3.5 9.2 0.3
HE1 A:HIS112 3.6 10.6 1.0
HD2 A:HIS452 3.6 11.9 1.0
O A:HOH605 3.6 19.2 1.0
HD2 A:HIS65 3.7 10.2 1.0
HE1 A:HIS110 3.7 8.8 1.0
CD2 A:HIS400 3.7 10.4 1.0
CU A:CU503 3.8 10.8 0.5
CU A:CU503 3.9 11.1 0.3
CD2 A:HIS65 3.9 11.3 1.0
NE2 A:HIS65 4.0 9.6 1.0
HD2 A:PHE450 4.0 12.1 1.0
ND1 A:HIS402 4.1 9.8 1.0
CG A:HIS112 4.2 10.5 1.0
CG A:HIS402 4.2 10.3 1.0
ND1 A:HIS452 4.3 12.0 1.0
ND1 A:HIS112 4.3 11.8 1.0
NE2 A:HIS400 4.3 13.1 1.0
HB3 A:PHE450 4.3 10.7 1.0
CE1 A:HIS110 4.4 8.9 1.0
CG A:HIS452 4.4 11.4 1.0
HB3 A:PRO80 4.5 10.9 1.0
CU A:CU502 4.5 10.8 0.7
NE2 A:HIS454 4.5 9.9 1.0
HD2 A:HIS454 4.5 10.4 1.0
CD2 A:HIS454 4.7 10.3 1.0
CG A:HIS65 4.7 8.9 1.0
CD2 A:PHE450 4.7 12.2 1.0
NE2 A:HIS110 4.8 7.7 1.0
CE1 A:HIS65 4.8 8.8 1.0
HD21 A:LEU459 4.9 13.2 1.0
HD1 A:HIS402 4.9 10.3 1.0
CG A:HIS400 4.9 10.9 1.0

Copper binding site 3 out of 7 in 6rhp

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Copper binding site 3 out of 7 in the Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).


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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:10.8
occ:0.65
 CU A:CU502 0.0 10.8 0.7
CU A:CU502 1.0 9.2 0.3
ND1 A:HIS67 1.8 10.1 1.0
NE2 A:HIS110 1.9 7.7 1.0
NE2 A:HIS454 2.2 9.9 1.0
O A:HOH603 2.7 2.3 0.3
HB2 A:HIS67 2.8 8.3 1.0
CE1 A:HIS67 2.8 9.8 1.0
CD2 A:HIS110 2.8 9.4 1.0
CG A:HIS67 2.9 8.8 1.0
CE1 A:HIS110 2.9 8.9 1.0
O1 A:OXY509 3.0 2.5 0.2
HD2 A:HIS110 3.0 9.0 1.0
HE1 A:HIS67 3.0 9.8 1.0
O2 A:OXY509 3.0 2.5 0.2
CE1 A:HIS454 3.0 11.0 1.0
HD2 A:HIS65 3.1 10.2 1.0
HE1 A:HIS454 3.1 10.6 1.0
O A:HOH601 3.2 10.5 0.3
HE1 A:HIS110 3.2 8.8 1.0
CD2 A:HIS454 3.3 10.3 1.0
HZ2 A:TRP108 3.3 10.4 1.0
CB A:HIS67 3.3 8.4 1.0
HD2 A:HIS454 3.5 10.4 1.0
HB2 A:ALA244 3.6 8.8 1.0
CZ2 A:TRP108 3.6 10.1 1.0
HE1 A:TRP108 3.8 10.6 1.0
CD2 A:HIS65 3.8 11.3 1.0
NE2 A:HIS67 3.9 9.6 1.0
CE2 A:TRP108 3.9 10.2 1.0
HB3 A:HIS67 3.9 8.3 1.0
CG A:HIS110 4.0 9.3 1.0
CD2 A:HIS67 4.0 9.4 1.0
ND1 A:HIS110 4.0 9.5 1.0
NE1 A:TRP108 4.0 10.8 1.0
CU A:CU503 4.1 10.8 0.5
CU A:CU503 4.1 11.1 0.3
ND1 A:HIS454 4.2 10.4 1.0
HA A:HIS67 4.2 8.2 1.0
NE2 A:HIS65 4.2 9.6 1.0
HD2 A:HIS400 4.3 11.1 1.0
CH2 A:TRP108 4.3 11.1 1.0
CG A:HIS454 4.4 11.1 1.0
HB1 A:ALA244 4.4 8.8 1.0
CB A:ALA244 4.4 8.9 1.0
CD2 A:HIS400 4.4 10.4 1.0
CA A:HIS67 4.4 7.8 1.0
CU A:CU501 4.5 5.7 0.3
HH2 A:TRP108 4.5 10.7 1.0
O A:HOH605 4.6 19.2 1.0
NE2 A:HIS400 4.6 13.1 1.0
HE2 A:HIS67 4.7 9.6 1.0
HD1 A:HIS110 4.8 9.3 1.0
CD2 A:TRP108 4.8 10.7 1.0
HB3 A:ALA244 4.8 8.8 1.0
HD2 A:HIS67 4.9 9.3 1.0
HD2 A:HIS112 4.9 10.1 1.0
HD1 A:HIS454 4.9 10.7 1.0
CD1 A:TRP108 5.0 10.5 1.0

Copper binding site 4 out of 7 in 6rhp

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Copper binding site 4 out of 7 in the Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).


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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:9.2
occ:0.30
 CU A:CU502 0.0 9.2 0.3
CU A:CU502 1.0 10.8 0.7
O A:HOH603 1.9 2.3 0.3
O1 A:OXY509 2.0 2.5 0.2
NE2 A:HIS454 2.1 9.9 1.0
ND1 A:HIS67 2.2 10.1 1.0
O2 A:OXY509 2.3 2.5 0.2
O A:HOH601 2.3 10.5 0.3
NE2 A:HIS110 2.3 7.7 1.0
HD2 A:HIS65 2.8 10.2 1.0
CE1 A:HIS67 2.9 9.8 1.0
HE1 A:HIS67 2.9 9.8 1.0
CD2 A:HIS454 3.0 10.3 1.0
HE1 A:HIS110 3.0 8.8 1.0
CE1 A:HIS110 3.0 8.9 1.0
HD2 A:HIS454 3.1 10.4 1.0
CE1 A:HIS454 3.2 11.0 1.0
CG A:HIS67 3.4 8.8 1.0
HD2 A:HIS400 3.4 11.1 1.0
HB2 A:HIS67 3.4 8.3 1.0
HE1 A:HIS454 3.4 10.6 1.0
CU A:CU501 3.5 5.7 0.3
CD2 A:HIS65 3.5 11.3 1.0
CD2 A:HIS110 3.5 9.4 1.0
CU A:CU503 3.5 10.8 0.5
CU A:CU503 3.5 11.1 0.3
CD2 A:HIS400 3.6 10.4 1.0
NE2 A:HIS65 3.8 9.6 1.0
HD2 A:HIS110 3.8 9.0 1.0
CB A:HIS67 3.9 8.4 1.0
NE2 A:HIS400 3.9 13.1 1.0
HB2 A:ALA244 4.1 8.8 1.0
O A:HOH605 4.1 19.2 1.0
NE2 A:HIS67 4.1 9.6 1.0
HZ2 A:TRP108 4.1 10.4 1.0
CG A:HIS454 4.2 11.1 1.0
ND1 A:HIS454 4.2 10.4 1.0
ND1 A:HIS110 4.3 9.5 1.0
HE1 A:HIS452 4.3 11.4 1.0
CU A:CU501 4.3 14.4 0.7
HA A:HIS67 4.3 8.2 1.0
CD2 A:HIS67 4.3 9.4 1.0
HD2 A:HIS112 4.4 10.1 1.0
CZ2 A:TRP108 4.5 10.1 1.0
CG A:HIS110 4.5 9.3 1.0
CG A:HIS400 4.6 10.9 1.0
HB3 A:HIS67 4.6 8.3 1.0
HE1 A:TRP108 4.7 10.6 1.0
CA A:HIS67 4.7 7.8 1.0
HB1 A:ALA244 4.8 8.8 1.0
CG A:HIS65 4.8 8.9 1.0
HE2 A:HIS67 4.8 9.6 1.0
CB A:ALA244 4.8 8.9 1.0
CE1 A:HIS452 4.9 11.0 1.0
NE2 A:HIS452 4.9 11.9 1.0
CE1 A:HIS400 4.9 12.4 1.0
CD2 A:HIS112 4.9 10.1 1.0
NE2 A:HIS112 4.9 9.5 1.0
CE2 A:TRP108 4.9 10.2 1.0
NE2 A:HIS402 4.9 8.8 1.0
NE1 A:TRP108 4.9 10.8 1.0
HD1 A:HIS110 5.0 9.3 1.0
HD1 A:HIS454 5.0 10.7 1.0

Copper binding site 5 out of 7 in 6rhp

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Copper binding site 5 out of 7 in the Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).


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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:11.1
occ:0.30
 CU A:CU503 0.0 11.1 0.3
CU A:CU503 0.0 10.8 0.5
O A:HOH973 1.8 3.0 0.3
NE2 A:HIS65 1.9 9.6 1.0
NE2 A:HIS400 2.0 13.1 1.0
O A:HOH603 2.0 2.3 0.3
O A:HOH973 2.7 5.6 0.7
CE1 A:HIS65 2.8 8.8 1.0
CD2 A:HIS400 2.9 10.4 1.0
HE1 A:HIS65 2.9 9.3 1.0
CE1 A:HIS400 3.0 12.4 1.0
HA A:HIS67 3.0 8.2 1.0
CD2 A:HIS65 3.0 11.3 1.0
HD2 A:HIS400 3.1 11.1 1.0
H A:GLY68 3.2 9.0 1.0
HE1 A:HIS400 3.2 12.6 1.0
HD2 A:HIS65 3.3 10.2 1.0
CD2 A:HIS402 3.4 9.3 1.0
O1 A:OXY509 3.4 2.5 0.2
NE2 A:HIS402 3.5 8.8 1.0
ND1 A:HIS67 3.5 10.1 1.0
CU A:CU502 3.5 9.2 0.3
HD2 A:HIS402 3.6 9.5 1.0
HA A:HIS402 3.6 10.7 1.0
CG A:HIS402 3.7 10.3 1.0
CG A:HIS67 3.8 8.8 1.0
CE1 A:HIS402 3.8 11.6 1.0
CE1 A:HIS67 3.8 9.8 1.0
CU A:CU501 3.9 5.7 0.3
CA A:HIS67 3.9 7.8 1.0
ND1 A:HIS402 3.9 9.8 1.0
ND1 A:HIS65 4.0 10.1 1.0
N A:GLY68 4.0 9.3 1.0
O A:HOH601 4.0 10.5 0.3
CG A:HIS400 4.1 10.9 1.0
ND1 A:HIS400 4.1 12.9 1.0
CG A:HIS65 4.1 8.9 1.0
CU A:CU502 4.1 10.8 0.7
HE1 A:HIS67 4.2 9.8 1.0
CB A:HIS67 4.2 8.4 1.0
HB2 A:HIS67 4.2 8.3 1.0
CD2 A:HIS67 4.3 9.4 1.0
HE1 A:HIS402 4.3 10.4 1.0
NE2 A:HIS67 4.3 9.6 1.0
CA A:HIS402 4.4 10.7 1.0
CU A:CU501 4.4 14.4 0.7
C A:HIS67 4.4 8.6 1.0
HD1 A:HIS402 4.4 10.3 1.0
CB A:HIS402 4.5 10.5 1.0
O2 A:OXY509 4.6 2.5 0.2
O A:HOH766 4.7 10.8 1.0
O A:HOH729 4.7 13.7 1.0
HD1 A:HIS65 4.7 9.5 1.0
HB3 A:HIS402 4.7 10.5 1.0
N A:HIS402 4.8 10.8 1.0
HD1 A:HIS400 4.9 12.2 1.0
HA2 A:GLY68 4.9 8.8 1.0
HE2 A:HIS67 4.9 9.6 1.0
HD2 A:HIS67 4.9 9.3 1.0
HD2 A:HIS112 4.9 10.1 1.0
O A:LEU401 4.9 10.7 1.0
N A:HIS67 5.0 8.4 1.0
O A:TRP66 5.0 9.0 1.0

Copper binding site 6 out of 7 in 6rhp

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Copper binding site 6 out of 7 in the Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).


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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:10.8
occ:0.52
 CU A:CU503 0.0 10.8 0.5
CU A:CU503 0.0 11.1 0.3
O A:HOH973 1.9 3.0 0.3
NE2 A:HIS65 1.9 9.6 1.0
NE2 A:HIS400 2.0 13.1 1.0
O A:HOH603 2.0 2.3 0.3
O A:HOH973 2.7 5.6 0.7
CE1 A:HIS65 2.8 8.8 1.0
CD2 A:HIS400 2.9 10.4 1.0
HE1 A:HIS65 2.9 9.3 1.0
HA A:HIS67 3.0 8.2 1.0
CD2 A:HIS65 3.0 11.3 1.0
CE1 A:HIS400 3.0 12.4 1.0
HD2 A:HIS400 3.1 11.1 1.0
H A:GLY68 3.2 9.0 1.0
HE1 A:HIS400 3.3 12.6 1.0
HD2 A:HIS65 3.3 10.2 1.0
CD2 A:HIS402 3.4 9.3 1.0
O1 A:OXY509 3.4 2.5 0.2
NE2 A:HIS402 3.5 8.8 1.0
ND1 A:HIS67 3.5 10.1 1.0
CU A:CU502 3.5 9.2 0.3
HD2 A:HIS402 3.6 9.5 1.0
HA A:HIS402 3.6 10.7 1.0
CG A:HIS402 3.7 10.3 1.0
CG A:HIS67 3.8 8.8 1.0
CE1 A:HIS402 3.8 11.6 1.0
CU A:CU501 3.8 5.7 0.3
CE1 A:HIS67 3.9 9.8 1.0
CA A:HIS67 3.9 7.8 1.0
ND1 A:HIS402 3.9 9.8 1.0
ND1 A:HIS65 3.9 10.1 1.0
N A:GLY68 4.0 9.3 1.0
O A:HOH601 4.0 10.5 0.3
CG A:HIS400 4.1 10.9 1.0
CG A:HIS65 4.1 8.9 1.0
ND1 A:HIS400 4.1 12.9 1.0
CU A:CU502 4.1 10.8 0.7
HE1 A:HIS67 4.2 9.8 1.0
CB A:HIS67 4.2 8.4 1.0
HB2 A:HIS67 4.2 8.3 1.0
HE1 A:HIS402 4.3 10.4 1.0
CD2 A:HIS67 4.3 9.4 1.0
NE2 A:HIS67 4.3 9.6 1.0
CU A:CU501 4.4 14.4 0.7
CA A:HIS402 4.4 10.7 1.0
HD1 A:HIS402 4.4 10.3 1.0
C A:HIS67 4.4 8.6 1.0
CB A:HIS402 4.5 10.5 1.0
O2 A:OXY509 4.6 2.5 0.2
O A:HOH766 4.7 10.8 1.0
HD1 A:HIS65 4.7 9.5 1.0
O A:HOH729 4.7 13.7 1.0
HB3 A:HIS402 4.8 10.5 1.0
N A:HIS402 4.8 10.8 1.0
HD1 A:HIS400 4.9 12.2 1.0
HA2 A:GLY68 4.9 8.8 1.0
HD2 A:HIS67 4.9 9.3 1.0
HE2 A:HIS67 4.9 9.6 1.0
HD2 A:HIS112 4.9 10.1 1.0
O A:LEU401 4.9 10.7 1.0
N A:HIS67 5.0 8.4 1.0
O A:TRP66 5.0 9.0 1.0

Copper binding site 7 out of 7 in 6rhp

Go back to Copper Binding Sites List in 6rhp
Copper binding site 7 out of 7 in the Single Crystal Serial Study of the X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing).


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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Twenty First Structure of the Series with 4415 Kgy Dose (Collected After Refreezing). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu504

b:10.6
occ:0.78
 ND1 A:HIS397 2.0 13.3 1.0
ND1 A:HIS458 2.0 14.4 1.0
SG A:CYS453 2.2 12.3 1.0
HD11 A:ILE455 2.6 13.9 1.0
CE1 A:HIS397 2.9 12.6 1.0
HB A:ILE455 3.0 13.3 1.0
HE1 A:HIS397 3.0 12.8 1.0
CE1 A:HIS458 3.0 12.2 1.0
CG A:HIS458 3.1 12.3 1.0
HD2 A:PHE463 3.1 11.6 1.0
HB2 A:HIS458 3.1 11.7 1.0
HB3 A:HIS397 3.1 12.8 1.0
CG A:HIS397 3.1 12.9 1.0
HE1 A:HIS458 3.2 12.8 1.0
HB3 A:HIS458 3.3 11.7 1.0
CB A:CYS453 3.3 11.6 1.0
HA A:HIS397 3.3 12.4 1.0
CB A:HIS458 3.4 11.5 1.0
HB2 A:CYS453 3.4 11.8 1.0
HB3 A:CYS453 3.4 11.8 1.0
CD1 A:ILE455 3.5 14.1 1.0
CB A:HIS397 3.5 12.8 1.0
HE2 A:PHE463 3.6 11.5 1.0
HD2 A:PRO398 3.8 10.6 1.0
HD12 A:ILE455 3.8 13.9 1.0
CB A:ILE455 3.8 13.8 1.0
CD2 A:PHE463 3.9 11.3 1.0
H A:ILE455 3.9 11.6 1.0
CA A:HIS397 3.9 12.5 1.0
CG1 A:ILE455 4.1 13.3 1.0
NE2 A:HIS397 4.1 12.5 1.0
HD13 A:ILE455 4.1 13.9 1.0
NE2 A:HIS458 4.1 13.0 1.0
CE2 A:PHE463 4.2 11.6 1.0
CD2 A:HIS458 4.2 12.3 1.0
HG13 A:ILE455 4.2 13.6 1.0
CD2 A:HIS397 4.2 13.2 1.0
HB2 A:HIS397 4.4 12.8 1.0
HG21 A:ILE455 4.4 14.0 1.0
HG22 A:ILE455 4.5 14.1 1.0
CG2 A:ILE455 4.6 14.2 1.0
HZ A:PHE341 4.6 14.1 1.0
CA A:CYS453 4.6 11.7 1.0
CD A:PRO398 4.6 10.4 1.0
CZ A:PHE341 4.7 14.0 1.0
O A:GLY394 4.7 16.1 1.0
N A:ILE455 4.8 11.5 1.0
HA A:CYS453 4.8 11.5 1.0
HE1 A:PHE399 4.8 11.7 1.0
HE2 A:HIS397 4.8 12.7 1.0
CA A:ILE455 4.9 11.7 1.0
HE2 A:PHE341 4.9 14.2 1.0
HD3 A:PRO398 4.9 10.6 1.0
C A:HIS397 4.9 11.7 1.0
CA A:HIS458 4.9 11.5 1.0
CE2 A:PHE341 4.9 14.4 1.0
HE2 A:HIS458 4.9 12.7 1.0
O A:ILE455 5.0 10.3 1.0
HB3 A:PHE463 5.0 12.2 1.0
HG12 A:ILE455 5.0 13.6 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 07:05:08 2024

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