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Copper in PDB 6rhh: 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. Third Structure of the Series with 315 Kgy Dose.

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. Third Structure of the Series with 315 Kgy Dose.

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. Third Structure of the Series with 315 Kgy Dose.:
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. Third Structure of the Series with 315 Kgy Dose., PDB code: 6rhh 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) 67.34 / 0.97
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.250, 84.130, 112.360, 90.00, 90.00, 90.00
R / Rfree (%) 11.5 / 13.1

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. Third Structure of the Series with 315 Kgy Dose. (pdb code 6rhh). 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. Third Structure of the Series with 315 Kgy Dose., PDB code: 6rhh:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7;

Copper binding site 1 out of 7 in 6rhh

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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. Third Structure of the Series with 315 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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Third Structure of the Series with 315 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:6.5
occ:0.44
CU A:CU501 0.0 6.5 0.4
CU A:CU501 0.8 7.9 0.5
O1 A:OXY509 1.6 7.2 0.1
O2 A:OXY509 1.8 7.5 0.1
O A:HOH601 1.8 9.2 0.5
NE2 A:HIS402 2.0 7.3 1.0
NE2 A:HIS112 2.2 8.1 1.0
NE2 A:HIS452 2.2 9.8 1.0
O A:HOH603 2.3 9.7 0.4
HD2 A:HIS400 2.9 5.5 1.0
CE1 A:HIS402 3.0 7.4 1.0
CE1 A:HIS452 3.1 9.3 1.0
CD2 A:HIS112 3.1 7.5 1.0
HE1 A:HIS402 3.1 6.2 1.0
HE1 A:HIS452 3.1 10.2 1.0
CD2 A:HIS402 3.1 7.2 1.0
HD2 A:HIS112 3.1 6.2 1.0
CE1 A:HIS112 3.3 8.7 1.0
HD2 A:HIS402 3.3 6.2 1.0
CD2 A:HIS452 3.4 9.3 1.0
CU A:CU502 3.5 9.5 0.4
HE1 A:HIS112 3.6 6.2 1.0
HD2 A:HIS452 3.6 10.3 1.0
HE1 A:HIS110 3.7 9.8 1.0
CU A:CU503 3.7 7.4 0.4
O A:HOH605 3.7 13.7 0.9
CD2 A:HIS400 3.7 7.7 1.0
HD2 A:HIS65 3.7 5.4 1.0
CU A:CU503 3.9 7.3 0.4
CD2 A:HIS65 3.9 7.9 1.0
HD2 A:PHE450 4.0 6.2 1.0
NE2 A:HIS65 4.0 8.0 1.0
ND1 A:HIS402 4.1 6.7 1.0
NE2 A:HIS400 4.2 7.9 1.0
CG A:HIS402 4.2 6.7 1.0
ND1 A:HIS452 4.3 8.5 1.0
HB3 A:PHE450 4.3 6.2 1.0
CG A:HIS112 4.3 7.3 1.0
ND1 A:HIS112 4.4 8.2 1.0
NE2 A:HIS454 4.4 7.3 1.0
CG A:HIS452 4.4 8.4 1.0
CE1 A:HIS110 4.4 7.6 1.0
HD2 A:HIS454 4.5 5.1 1.0
CU A:CU502 4.5 6.4 0.5
HB3 A:PRO80 4.6 5.1 1.0
CD2 A:HIS454 4.6 7.2 1.0
CD2 A:PHE450 4.7 8.1 1.0
CG A:HIS65 4.7 7.4 1.0
NE2 A:HIS110 4.8 7.9 1.0
CE1 A:HIS65 4.8 7.5 1.0
HD21 A:LEU459 4.8 7.3 1.0
HD1 A:HIS402 4.9 6.2 1.0
CG A:HIS400 5.0 7.6 1.0
HD1 A:HIS452 5.0 10.3 1.0

Copper binding site 2 out of 7 in 6rhh

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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. Third Structure of the Series with 315 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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Third Structure of the Series with 315 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:7.9
occ:0.51
CU A:CU501 0.0 7.9 0.5
CU A:CU501 0.8 6.5 0.4
NE2 A:HIS452 1.9 9.8 1.0
NE2 A:HIS402 2.0 7.3 1.0
NE2 A:HIS112 2.0 8.1 1.0
O2 A:OXY509 2.3 7.5 0.1
O1 A:OXY509 2.4 7.2 0.1
O A:HOH601 2.5 9.2 0.5
CD2 A:HIS452 2.8 9.3 1.0
CE1 A:HIS112 2.9 8.7 1.0
CE1 A:HIS402 2.9 7.4 1.0
CE1 A:HIS452 2.9 9.3 1.0
HE1 A:HIS112 3.0 6.2 1.0
HD2 A:HIS452 3.0 10.3 1.0
HE1 A:HIS402 3.0 6.2 1.0
CD2 A:HIS402 3.1 7.2 1.0
CD2 A:HIS112 3.1 7.5 1.0
O A:HOH603 3.1 9.7 0.4
HE1 A:HIS452 3.2 10.2 1.0
HD2 A:PHE450 3.2 6.2 1.0
HD2 A:HIS402 3.3 6.2 1.0
HD2 A:HIS112 3.4 6.2 1.0
HD2 A:HIS400 3.4 5.5 1.0
HB3 A:PHE450 3.6 6.2 1.0
CD2 A:PHE450 3.9 8.1 1.0
O A:HOH605 3.9 13.7 0.9
CG A:HIS452 4.0 8.4 1.0
ND1 A:HIS452 4.0 8.5 1.0
ND1 A:HIS402 4.0 6.7 1.0
ND1 A:HIS112 4.0 8.2 1.0
HB3 A:PRO80 4.1 5.1 1.0
CG A:HIS402 4.2 6.7 1.0
HE1 A:HIS110 4.2 9.8 1.0
CG A:HIS112 4.2 7.3 1.0
CD2 A:HIS400 4.2 7.7 1.0
CU A:CU503 4.3 7.4 0.4
CU A:CU502 4.3 9.5 0.4
CB A:PHE450 4.4 7.5 1.0
HD2 A:HIS65 4.4 5.4 1.0
HD21 A:LEU459 4.4 7.3 1.0
HB2 A:PHE450 4.5 6.2 1.0
CU A:CU503 4.6 7.3 0.4
CD2 A:HIS65 4.6 7.9 1.0
CG A:PHE450 4.6 7.3 1.0
NE2 A:HIS65 4.6 8.0 1.0
HE2 A:PHE450 4.6 6.2 1.0
CE2 A:PHE450 4.7 9.3 1.0
NE2 A:HIS400 4.8 7.9 1.0
HD1 A:HIS452 4.8 10.3 1.0
HD1 A:HIS402 4.8 6.2 1.0
HD1 A:HIS112 4.8 6.2 1.0
HD22 A:LEU459 4.9 7.3 1.0

Copper binding site 3 out of 7 in 6rhh

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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. Third Structure of the Series with 315 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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Third Structure of the Series with 315 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:9.5
occ:0.44
CU A:CU502 0.0 9.5 0.4
CU A:CU502 1.0 6.4 0.5
O1 A:OXY509 1.9 7.2 0.1
NE2 A:HIS454 1.9 7.3 1.0
O A:HOH603 2.0 9.7 0.4
O A:HOH601 2.1 9.2 0.5
ND1 A:HIS67 2.2 7.7 1.0
NE2 A:HIS110 2.3 7.9 1.0
O2 A:OXY509 2.6 7.5 0.1
CD2 A:HIS454 2.9 7.2 1.0
HD2 A:HIS65 3.0 5.4 1.0
CE1 A:HIS454 3.0 7.2 1.0
CE1 A:HIS110 3.0 7.6 1.0
HE1 A:HIS110 3.0 9.8 1.0
CE1 A:HIS67 3.0 7.0 1.0
HD2 A:HIS454 3.1 5.1 1.0
HE1 A:HIS67 3.1 5.1 1.0
HE1 A:HIS454 3.2 5.1 1.0
HB2 A:HIS67 3.3 5.0 1.0
CG A:HIS67 3.3 7.3 1.0
CD2 A:HIS110 3.5 7.7 1.0
HD2 A:HIS400 3.5 5.5 1.0
CU A:CU501 3.5 6.5 0.4
CU A:CU503 3.6 7.4 0.4
CD2 A:HIS65 3.7 7.9 1.0
CU A:CU503 3.7 7.3 0.4
CD2 A:HIS400 3.8 7.7 1.0
HD2 A:HIS110 3.8 9.9 1.0
CB A:HIS67 3.8 7.1 1.0
NE2 A:HIS400 3.9 7.9 1.0
HB2 A:ALA244 4.0 5.5 1.0
NE2 A:HIS65 4.1 8.0 1.0
O A:HOH605 4.1 13.7 0.9
ND1 A:HIS454 4.1 7.0 1.0
CG A:HIS454 4.1 7.0 1.0
HZ2 A:TRP108 4.1 5.5 1.0
HE1 A:HIS452 4.2 10.2 1.0
NE2 A:HIS67 4.2 7.7 1.0
ND1 A:HIS110 4.3 7.3 1.0
CU A:CU501 4.3 7.9 0.5
HA A:HIS67 4.4 4.4 1.0
CD2 A:HIS67 4.4 7.4 1.0
HD2 A:HIS112 4.5 6.2 1.0
CG A:HIS110 4.5 7.3 1.0
CZ2 A:TRP108 4.5 6.9 1.0
HB3 A:HIS67 4.5 5.0 1.0
HB1 A:ALA244 4.6 5.5 1.0
CG A:HIS400 4.7 7.6 1.0
HE1 A:TRP108 4.7 5.5 1.0
CB A:ALA244 4.7 6.9 1.0
CA A:HIS67 4.8 6.5 1.0
CE1 A:HIS400 4.8 7.4 1.0
CE2 A:TRP108 4.8 6.7 1.0
CE1 A:HIS452 4.8 9.3 1.0
HD1 A:HIS454 4.9 5.1 1.0
NE2 A:HIS452 4.9 9.8 1.0
NE1 A:TRP108 4.9 6.9 1.0
NE2 A:HIS112 4.9 8.1 1.0
CG A:HIS65 5.0 7.4 1.0
NE2 A:HIS402 5.0 7.3 1.0
HE2 A:HIS67 5.0 5.1 1.0
CD2 A:HIS112 5.0 7.5 1.0
HD1 A:HIS110 5.0 9.9 1.0

Copper binding site 4 out of 7 in 6rhh

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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. Third Structure of the Series with 315 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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Third Structure of the Series with 315 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:6.4
occ:0.51
CU A:CU502 0.0 6.4 0.5
CU A:CU502 1.0 9.5 0.4
ND1 A:HIS67 1.8 7.7 1.0
NE2 A:HIS110 1.9 7.9 1.0
NE2 A:HIS454 2.2 7.3 1.0
HB2 A:HIS67 2.7 5.0 1.0
CG A:HIS67 2.8 7.3 1.0
CD2 A:HIS110 2.9 7.7 1.0
O A:HOH603 2.9 9.7 0.4
O1 A:OXY509 2.9 7.2 0.1
CE1 A:HIS67 2.9 7.0 1.0
CE1 A:HIS454 3.0 7.2 1.0
HD2 A:HIS110 3.0 9.9 1.0
CE1 A:HIS110 3.0 7.6 1.0
O A:HOH601 3.0 9.2 0.5
HE1 A:HIS454 3.0 5.1 1.0
HE1 A:HIS67 3.1 5.1 1.0
HD2 A:HIS65 3.2 5.4 1.0
CB A:HIS67 3.2 7.1 1.0
CD2 A:HIS454 3.3 7.2 1.0
HE1 A:HIS110 3.3 9.8 1.0
HZ2 A:TRP108 3.4 5.5 1.0
O2 A:OXY509 3.5 7.5 0.1
HB2 A:ALA244 3.5 5.5 1.0
HD2 A:HIS454 3.6 5.1 1.0
CZ2 A:TRP108 3.7 6.9 1.0
HB3 A:HIS67 3.8 5.0 1.0
HE1 A:TRP108 3.8 5.5 1.0
CE2 A:TRP108 3.9 6.7 1.0
NE1 A:TRP108 4.0 6.9 1.0
NE2 A:HIS67 4.0 7.7 1.0
CD2 A:HIS67 4.0 7.4 1.0
CD2 A:HIS65 4.0 7.9 1.0
CG A:HIS110 4.0 7.3 1.0
ND1 A:HIS110 4.1 7.3 1.0
CU A:CU503 4.1 7.4 0.4
ND1 A:HIS454 4.2 7.0 1.0
HA A:HIS67 4.2 4.4 1.0
CU A:CU503 4.2 7.3 0.4
HB1 A:ALA244 4.3 5.5 1.0
CB A:ALA244 4.3 6.9 1.0
CG A:HIS454 4.4 7.0 1.0
HD2 A:HIS400 4.4 5.5 1.0
CH2 A:TRP108 4.4 7.3 1.0
CA A:HIS67 4.4 6.5 1.0
NE2 A:HIS65 4.5 8.0 1.0
NE2 A:HIS400 4.5 7.9 1.0
CU A:CU501 4.5 6.5 0.4
CD2 A:HIS400 4.5 7.7 1.0
HH2 A:TRP108 4.6 5.6 1.0
O A:HOH605 4.6 13.7 0.9
HB3 A:ALA244 4.7 5.5 1.0
CD2 A:TRP108 4.8 6.8 1.0
HE2 A:HIS67 4.8 5.1 1.0
HD2 A:HIS67 4.8 5.1 1.0
HD1 A:HIS110 4.9 9.9 1.0
CD1 A:TRP108 4.9 6.9 1.0
HD1 A:HIS454 4.9 5.1 1.0

Copper binding site 5 out of 7 in 6rhh

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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. Third Structure of the Series with 315 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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Third Structure of the Series with 315 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:7.4
occ:0.44
CU A:CU503 0.0 7.4 0.4
CU A:CU503 0.2 7.3 0.4
NE2 A:HIS400 1.9 7.9 1.0
O A:HOH603 1.9 9.7 0.4
NE2 A:HIS65 1.9 8.0 1.0
O A:HOH1094 2.1 6.3 0.4
O A:HOH1094 2.6 6.2 0.6
CD2 A:HIS400 2.9 7.7 1.0
CE1 A:HIS65 2.9 7.5 1.0
CE1 A:HIS400 2.9 7.4 1.0
CD2 A:HIS65 3.0 7.9 1.0
HD2 A:HIS400 3.0 5.5 1.0
HA A:HIS67 3.0 4.4 1.0
HE1 A:HIS65 3.1 5.4 1.0
HE1 A:HIS400 3.2 5.5 1.0
HD2 A:HIS65 3.2 5.4 1.0
H A:GLY68 3.2 4.4 1.0
CD2 A:HIS402 3.3 7.2 1.0
O1 A:OXY509 3.3 7.2 0.1
NE2 A:HIS402 3.4 7.3 1.0
HD2 A:HIS402 3.4 6.2 1.0
ND1 A:HIS67 3.5 7.7 1.0
CU A:CU502 3.6 9.5 0.4
HA A:HIS402 3.6 5.0 1.0
CG A:HIS402 3.7 6.7 1.0
CU A:CU501 3.7 6.5 0.4
CE1 A:HIS402 3.8 7.4 1.0
CG A:HIS67 3.8 7.3 1.0
CA A:HIS67 3.9 6.5 1.0
ND1 A:HIS402 3.9 6.7 1.0
CE1 A:HIS67 3.9 7.0 1.0
O A:HOH601 4.0 9.2 0.5
CG A:HIS400 4.0 7.6 1.0
ND1 A:HIS400 4.0 7.3 1.0
ND1 A:HIS65 4.0 7.3 1.0
N A:GLY68 4.1 6.5 1.0
CU A:CU502 4.1 6.4 0.5
CG A:HIS65 4.1 7.4 1.0
HB2 A:HIS67 4.2 5.0 1.0
CB A:HIS67 4.2 7.1 1.0
HE1 A:HIS67 4.2 5.1 1.0
HE1 A:HIS402 4.3 6.2 1.0
CU A:CU501 4.3 7.9 0.5
CD2 A:HIS67 4.4 7.4 1.0
CA A:HIS402 4.4 6.8 1.0
NE2 A:HIS67 4.4 7.7 1.0
O2 A:OXY509 4.5 7.5 0.1
HD1 A:HIS402 4.5 6.2 1.0
CB A:HIS402 4.5 7.0 1.0
C A:HIS67 4.5 6.9 1.0
O A:HOH791 4.7 12.8 1.0
O A:HOH996 4.7 12.4 1.0
HB3 A:HIS402 4.7 6.2 1.0
N A:HIS402 4.8 6.7 1.0
HD1 A:HIS65 4.8 5.4 1.0
HD1 A:HIS400 4.8 5.5 1.0
HA2 A:GLY68 4.9 5.3 1.0
HD2 A:HIS112 4.9 6.2 1.0
HD2 A:HIS67 4.9 5.1 1.0
N A:HIS67 5.0 6.5 1.0
O A:LEU401 5.0 7.5 1.0
HE2 A:HIS67 5.0 5.1 1.0
HD2 A:HIS454 5.0 5.1 1.0

Copper binding site 6 out of 7 in 6rhh

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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. Third Structure of the Series with 315 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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Third Structure of the Series with 315 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu503

b:7.3
occ:0.38
CU A:CU503 0.0 7.3 0.4
CU A:CU503 0.2 7.4 0.4
O A:HOH1094 1.8 6.3 0.4
NE2 A:HIS65 1.9 8.0 1.0
NE2 A:HIS400 1.9 7.9 1.0
O A:HOH603 2.1 9.7 0.4
O A:HOH1094 2.4 6.2 0.6
CE1 A:HIS65 2.8 7.5 1.0
HA A:HIS67 2.9 4.4 1.0
CE1 A:HIS400 2.9 7.4 1.0
HE1 A:HIS65 3.0 5.4 1.0
H A:GLY68 3.0 4.4 1.0
CD2 A:HIS400 3.0 7.7 1.0
CD2 A:HIS65 3.0 7.9 1.0
HE1 A:HIS400 3.1 5.5 1.0
HD2 A:HIS400 3.3 5.5 1.0
HD2 A:HIS65 3.3 5.4 1.0
CD2 A:HIS402 3.4 7.2 1.0
NE2 A:HIS402 3.5 7.3 1.0
HA A:HIS402 3.5 5.0 1.0
O1 A:OXY509 3.5 7.2 0.1
HD2 A:HIS402 3.6 6.2 1.0
ND1 A:HIS67 3.6 7.7 1.0
CG A:HIS402 3.7 6.7 1.0
CU A:CU502 3.7 9.5 0.4
CG A:HIS67 3.8 7.3 1.0
CA A:HIS67 3.8 6.5 1.0
N A:GLY68 3.8 6.5 1.0
CE1 A:HIS402 3.9 7.4 1.0
CU A:CU501 3.9 6.5 0.4
ND1 A:HIS402 4.0 6.7 1.0
ND1 A:HIS65 4.0 7.3 1.0
CE1 A:HIS67 4.0 7.0 1.0
ND1 A:HIS400 4.1 7.3 1.0
CG A:HIS65 4.1 7.4 1.0
CG A:HIS400 4.1 7.6 1.0
HB2 A:HIS67 4.1 5.0 1.0
CB A:HIS67 4.1 7.1 1.0
CU A:CU502 4.2 6.4 0.5
O A:HOH601 4.3 9.2 0.5
CD2 A:HIS67 4.3 7.4 1.0
CA A:HIS402 4.3 6.8 1.0
C A:HIS67 4.3 6.9 1.0
HE1 A:HIS67 4.4 5.1 1.0
HE1 A:HIS402 4.4 6.2 1.0
NE2 A:HIS67 4.4 7.7 1.0
CB A:HIS402 4.5 7.0 1.0
O A:HOH791 4.5 12.8 1.0
HD1 A:HIS402 4.5 6.2 1.0
O A:HOH996 4.5 12.4 1.0
CU A:CU501 4.6 7.9 0.5
HB3 A:HIS402 4.6 6.2 1.0
HA2 A:GLY68 4.7 5.3 1.0
O2 A:OXY509 4.7 7.5 0.1
HD1 A:HIS65 4.7 5.4 1.0
N A:HIS402 4.8 6.7 1.0
HD2 A:HIS67 4.8 5.1 1.0
N A:HIS67 4.8 6.5 1.0
HD1 A:HIS400 4.8 5.5 1.0
O A:TRP66 4.9 6.8 1.0
CA A:GLY68 4.9 6.7 1.0
O A:LEU401 4.9 7.5 1.0
HE2 A:HIS67 5.0 5.1 1.0

Copper binding site 7 out of 7 in 6rhh

Go back to Copper Binding Sites List in 6rhh
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. Third Structure of the Series with 315 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 X-Ray Induced Enzymatic Reduction of Molecular Oxygen to Water For Laccase From Steccherinum Murashkinskyi at Sub-Atomic Resolution. Third Structure of the Series with 315 Kgy Dose. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu504

b:7.0
occ:0.78
ND1 A:HIS458 2.0 8.1 1.0
ND1 A:HIS397 2.0 8.3 1.0
SG A:CYS453 2.2 8.6 1.0
HD11 A:ILE455 2.6 6.1 1.0
HB A:ILE455 3.0 6.1 1.0
CE1 A:HIS397 3.0 8.4 1.0
CE1 A:HIS458 3.0 8.8 1.0
CG A:HIS458 3.1 8.1 1.0
HD2 A:PHE463 3.1 8.9 1.0
CG A:HIS397 3.1 8.3 1.0
HB3 A:HIS397 3.1 8.4 1.0
HE1 A:HIS397 3.1 6.6 1.0
HB2 A:HIS458 3.1 6.1 1.0
HE1 A:HIS458 3.2 7.0 1.0
HB3 A:HIS458 3.3 6.1 1.0
CB A:CYS453 3.3 7.8 1.0
HA A:HIS397 3.4 6.1 1.0
CB A:HIS458 3.4 8.0 1.0
HB2 A:CYS453 3.4 5.8 1.0
HB3 A:CYS453 3.4 5.8 1.0
CB A:HIS397 3.5 8.1 1.0
HE2 A:PHE463 3.5 8.9 1.0
CD1 A:ILE455 3.6 8.1 1.0
HD2 A:PRO398 3.8 6.1 1.0
CD2 A:PHE463 3.8 8.1 1.0
CB A:ILE455 3.8 7.7 1.0
H A:ILE455 3.9 6.1 1.0
HD12 A:ILE455 4.0 6.1 1.0
CA A:HIS397 4.0 7.6 1.0
CE2 A:PHE463 4.1 8.4 1.0
CG1 A:ILE455 4.1 7.9 1.0
NE2 A:HIS397 4.1 8.8 1.0
HG13 A:ILE455 4.1 6.1 1.0
NE2 A:HIS458 4.1 8.9 1.0
HD13 A:ILE455 4.2 6.1 1.0
CD2 A:HIS458 4.2 8.7 1.0
CD2 A:HIS397 4.2 9.0 1.0
HB2 A:HIS397 4.4 8.4 1.0
HG21 A:ILE455 4.5 6.1 1.0
HZ A:PHE341 4.6 17.2 1.0
CD A:PRO398 4.6 7.6 1.0
HG22 A:ILE455 4.6 6.1 1.0
CG2 A:ILE455 4.6 7.9 1.0
CA A:CYS453 4.7 7.0 1.0
O A:GLY394 4.7 11.9 1.0
CZ A:PHE341 4.7 10.1 1.0
N A:ILE455 4.7 7.5 1.0
HD3 A:PRO398 4.8 6.1 1.0
HE1 A:PHE399 4.8 8.1 1.0
HA A:CYS453 4.8 5.2 1.0
HE2 A:HIS397 4.9 6.6 1.0
CA A:ILE455 4.9 7.7 1.0
HE2 A:PHE341 4.9 17.2 1.0
CA A:HIS458 4.9 8.3 1.0
CE2 A:PHE341 4.9 9.9 1.0
HE2 A:HIS458 4.9 7.0 1.0
O A:ILE455 4.9 7.9 1.0
C A:HIS397 4.9 7.2 1.0
HA2 A:GLY395 5.0 8.4 1.0
HB3 A:PHE463 5.0 6.7 1.0
N A:HIS397 5.0 7.9 1.0
HG12 A:ILE455 5.0 6.1 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: Sun Dec 13 11:25:18 2020

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