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Copper in PDB 6qq1: Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii

Enzymatic activity of Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii

All present enzymatic activity of Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii:
1.7.2.1;

Protein crystallography data

The structure of Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii, PDB code: 6qq1 was solved by S.V.Antonyuk, R.T.Shenoy, T.M.Hedison, R.R.Eady, S.S.Hasnain, N.S.Scrutton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 65.10 / 1.75
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 128.291, 128.291, 86.177, 90.00, 90.00, 120.00
R / Rfree (%) 13.6 / 16.3

Other elements in 6qq1:

The structure of Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii also contains other interesting chemical elements:

Iron (Fe) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii (pdb code 6qq1). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii, PDB code: 6qq1:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 6qq1

Go back to Copper Binding Sites List in 6qq1
Copper binding site 1 out of 2 in the Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:17.0
occ:1.00
ND1 A:HIS94 2.0 14.1 1.0
ND1 A:HIS143 2.1 15.8 1.0
SG A:CYS135 2.2 17.1 1.0
SD A:MET148 2.6 17.7 1.0
CE1 A:HIS143 2.9 15.1 1.0
CE1 A:HIS94 2.9 13.8 1.0
CG A:HIS94 3.1 14.2 1.0
CG A:HIS143 3.1 14.8 1.0
CB A:CYS135 3.2 15.1 1.0
CE A:MET148 3.5 18.2 1.0
CB A:HIS94 3.5 15.4 1.0
CB A:HIS143 3.5 14.6 1.0
CA A:HIS94 3.7 14.8 1.0
NE2 A:HIS143 4.1 15.8 1.0
O A:PRO93 4.1 14.5 1.0
NE2 A:HIS94 4.1 14.9 1.0
CG A:MET148 4.1 15.7 1.0
CD2 A:HIS143 4.2 16.0 1.0
CD2 A:HIS94 4.2 14.3 1.0
OG1 A:THR137 4.4 20.3 1.0
CB A:THR137 4.4 17.9 1.0
CE3 A:TRP61 4.5 14.3 1.0
CA A:HIS143 4.6 13.5 1.0
N A:ASN95 4.6 15.7 1.0
CB A:MET148 4.6 14.0 1.0
CA A:CYS135 4.6 14.8 1.0
N A:HIS94 4.7 15.2 1.0
C A:HIS94 4.8 16.2 1.0
C A:PRO93 4.8 15.6 1.0

Copper binding site 2 out of 2 in 6qq1

Go back to Copper Binding Sites List in 6qq1
Copper binding site 2 out of 2 in the Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of As Isolated Y323F Mutant of Haem-Cu Containing Nitrite Reductase From Ralstonia Pickettii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:17.1
occ:1.00
O A:HOH610 1.9 20.8 1.0
NE2 A:HIS134 2.0 15.0 1.0
NE2 A:HIS99 2.0 15.7 1.0
CD2 A:HIS134 2.9 15.2 1.0
CE1 A:HIS99 3.0 16.0 1.0
CD2 A:HIS99 3.0 14.9 1.0
CE1 A:HIS134 3.1 16.9 1.0
OD2 A:ASP97 3.6 24.2 0.8
ND1 A:HIS99 4.1 16.6 1.0
CG A:HIS134 4.1 14.8 1.0
CG A:HIS99 4.2 15.4 1.0
ND1 A:HIS134 4.2 16.9 1.0
CG A:ASP97 4.3 19.6 0.8
O A:HOH812 4.4 13.5 0.2
OD1 A:ASP97 4.6 21.2 0.8

Reference:

T.M.Hedison, R.T.Shenoy, A.I.Iorgu, D.J.Heyes, K.Fisher, G.Wright, S.Hay, R.R.Eady, S.S.Hasnain, N.S.Scrutton. Unexpected Roles of A Tether Harboring A Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis Acs Catalysis 2019.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.9B01266
Page generated: Wed Jul 31 06:50:47 2024

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