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Copper in PDB 6y72: Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A

Enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A

All present enzymatic activity of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A:
1.7.2.4;

Protein crystallography data

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A, PDB code: 6y72 was solved by L.Zhang, P.M.H.Kroneck, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 76.45 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 68.741, 76.453, 108.761, 90, 93.32, 90
R / Rfree (%) 16.1 / 20.5

Other elements in 6y72:

The structure of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A also contains other interesting chemical elements:

Sodium (Na) 2 atoms
Chlorine (Cl) 1 atom
Potassium (K) 1 atom
Calcium (Ca) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A (pdb code 6y72). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A, PDB code: 6y72:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 6y72

Go back to Copper Binding Sites List in 6y72
Copper binding site 1 out of 4 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu710

b:30.0
occ:1.00
CU1 A:CUA710 0.0 30.0 1.0
ND1 A:HIS583 2.3 27.9 1.0
SG A:CYS618 2.4 17.7 0.8
SD A:MET629 2.4 24.9 1.0
SG A:CYS622 2.6 24.9 1.0
CU2 A:CUA710 2.7 31.7 1.0
CE A:MET629 3.2 25.4 1.0
CE1 A:HIS583 3.2 28.0 1.0
CB A:CYS618 3.3 20.4 1.0
CG A:HIS583 3.3 25.9 1.0
CB A:CYS622 3.4 26.1 1.0
CB A:HIS583 3.7 20.1 1.0
CG A:MET629 3.8 19.7 1.0
CA A:HIS583 4.0 16.6 1.0
O A:TRP620 4.0 22.3 1.0
NE2 A:HIS583 4.4 24.5 1.0
CB A:MET629 4.4 21.0 1.0
CD2 A:HIS583 4.4 22.5 1.0
O A:SER582 4.6 18.8 1.0
CA A:CYS618 4.7 18.7 1.0
ND1 A:HIS626 4.7 28.8 1.0
N A:GLY584 4.7 20.7 1.0
CA A:CYS622 4.8 26.6 1.0
C A:HIS583 5.0 17.9 1.0
N A:HIS583 5.0 16.9 1.0

Copper binding site 2 out of 4 in 6y72

Go back to Copper Binding Sites List in 6y72
Copper binding site 2 out of 4 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu710

b:31.7
occ:1.00
CU2 A:CUA710 0.0 31.7 1.0
ND1 A:HIS626 2.1 28.8 1.0
O A:TRP620 2.5 22.3 1.0
SG A:CYS622 2.5 24.9 1.0
SG A:CYS618 2.6 17.7 0.8
CU1 A:CUA710 2.7 30.0 1.0
CE1 A:HIS626 3.0 30.6 1.0
CG A:HIS626 3.2 28.1 1.0
CB A:CYS622 3.3 26.1 1.0
N A:CYS622 3.4 27.1 1.0
CB A:CYS618 3.5 20.4 1.0
C A:TRP620 3.5 17.7 1.0
CB A:HIS626 3.6 28.1 1.0
CA A:HIS626 3.9 28.7 1.0
CA A:CYS622 4.0 26.6 1.0
CA A:PHE621 4.0 25.1 1.0
C A:PHE621 4.0 31.1 1.0
NE2 A:HIS626 4.1 29.6 1.0
N A:PHE621 4.1 23.9 1.0
O A:CYS618 4.2 21.0 1.0
O A:HIS626 4.2 30.2 1.0
CD2 A:HIS626 4.2 32.4 1.0
SD A:MET629 4.3 24.9 1.0
N A:TRP620 4.4 19.8 1.0
C A:CYS618 4.4 20.3 1.0
C A:HIS626 4.5 27.5 1.0
CA A:TRP620 4.5 16.3 1.0
CA A:CYS618 4.6 18.7 1.0
ND1 A:HIS583 4.7 27.9 1.0
CB A:MET629 4.7 21.0 1.0
C A:CYS622 4.8 30.7 1.0
O A:HOH924 4.9 25.6 1.0
N A:HIS623 5.0 27.9 1.0

Copper binding site 3 out of 4 in 6y72

Go back to Copper Binding Sites List in 6y72
Copper binding site 3 out of 4 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu707

b:35.1
occ:1.00
CU1 B:CUA707 0.0 35.1 1.0
SG B:CYS618 2.5 18.1 0.8
ND1 B:HIS583 2.5 33.0 1.0
SD B:MET629 2.5 28.5 1.0
SG B:CYS622 2.6 19.0 0.7
CU2 B:CUA707 2.7 35.4 1.0
CE B:MET629 3.2 29.1 1.0
CB B:CYS618 3.2 25.6 1.0
CB B:CYS622 3.3 24.4 1.0
CE1 B:HIS583 3.3 32.5 1.0
CG B:HIS583 3.4 28.2 1.0
CB B:HIS583 3.7 21.9 1.0
CG B:MET629 3.9 25.2 1.0
CA B:HIS583 4.0 21.5 1.0
O B:TRP620 4.0 26.6 1.0
CB B:MET629 4.3 23.0 1.0
NE2 B:HIS583 4.5 30.1 1.0
CD2 B:HIS583 4.5 30.1 1.0
O B:SER582 4.6 20.3 1.0
CA B:CYS618 4.7 19.7 1.0
CA B:CYS622 4.7 34.6 1.0
ND1 B:HIS626 4.7 29.5 1.0
N B:GLY584 4.8 20.3 1.0
N B:CYS622 4.9 31.6 1.0

Copper binding site 4 out of 4 in 6y72

Go back to Copper Binding Sites List in 6y72
Copper binding site 4 out of 4 in the Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Pseudomonas Stutzeri Nitrous Oxide Reductase Mutant, H178A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu707

b:35.4
occ:1.00
CU2 B:CUA707 0.0 35.4 1.0
ND1 B:HIS626 2.1 29.5 1.0
O B:TRP620 2.5 26.6 1.0
SG B:CYS622 2.6 19.0 0.7
SG B:CYS618 2.6 18.1 0.8
CU1 B:CUA707 2.7 35.1 1.0
CG B:HIS626 3.0 31.3 1.0
CE1 B:HIS626 3.1 25.1 1.0
N B:CYS622 3.3 31.6 1.0
CB B:CYS622 3.3 24.4 1.0
CB B:HIS626 3.3 34.8 1.0
C B:TRP620 3.5 23.8 1.0
CB B:CYS618 3.5 25.6 1.0
CA B:HIS626 3.9 38.7 1.0
CA B:CYS622 3.9 34.6 1.0
CA B:PHE621 4.0 29.9 1.0
C B:PHE621 4.0 30.7 1.0
N B:PHE621 4.2 26.6 1.0
CD2 B:HIS626 4.2 31.5 1.0
NE2 B:HIS626 4.2 30.8 1.0
O B:CYS618 4.2 19.9 1.0
O B:HIS626 4.2 26.8 1.0
N B:TRP620 4.4 23.1 1.0
C B:HIS626 4.4 38.4 1.0
C B:CYS618 4.4 19.9 1.0
SD B:MET629 4.5 28.5 1.0
CA B:TRP620 4.5 21.7 1.0
CA B:CYS618 4.6 19.7 1.0
ND1 B:HIS583 4.8 33.0 1.0
CB B:MET629 4.8 23.0 1.0
C B:CYS622 4.8 35.3 1.0
O B:HOH877 4.8 27.5 1.0
N B:HIS623 4.9 37.0 1.0

Reference:

L.Zhang, E.Bill, P.M.H.Kroneck, O.Einsle. A [3CU:2S] Cluster Provides Insight Into the Assembly and Function of the Cuz Site of Nitrous Oxide Reductase Chem Sci 2021.
ISSN: ESSN 2041-6539
DOI: 10.1039/D0SC05204C
Page generated: Mon Jul 14 07:31:24 2025

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