Atomistry » Copper » PDB 4b61-4e9t » 4csp
Atomistry »
  Copper »
    PDB 4b61-4e9t »
      4csp »

Copper in PDB 4csp: Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans

Enzymatic activity of Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans

All present enzymatic activity of Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans:
1.7.2.1;

Protein crystallography data

The structure of Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans, PDB code: 4csp was solved by N.G.H.Leferink, S.V.Antonyuk, J.A.Houwman, N.S.Scrutton, R.Ready, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.47 / 1.70
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 89.990, 89.990, 289.450, 90.00, 90.00, 120.00
R / Rfree (%) 18.112 / 21.482

Other elements in 4csp:

The structure of Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans (pdb code 4csp). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans, PDB code: 4csp:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 4csp

Go back to Copper Binding Sites List in 4csp
Copper binding site 1 out of 4 in the Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:21.1
occ:1.00
 ND1 A:HIS139 2.1 20.3 1.0
ND1 A:HIS89 2.1 20.0 1.0
SG A:CYS130 2.2 20.8 1.0
SD A:MET144 2.6 22.0 1.0
CE1 A:HIS139 3.0 21.1 1.0
CE1 A:HIS89 3.0 19.9 1.0
CG A:HIS139 3.1 20.3 1.0
CB A:CYS130 3.2 20.4 1.0
CG A:HIS89 3.2 21.4 1.0
CE A:MET144 3.5 21.2 1.0
CB A:HIS139 3.5 18.1 1.0
CB A:HIS89 3.6 20.7 1.0
CA A:HIS89 3.9 21.3 1.0
CG A:PRO132 3.9 23.7 1.0
NE2 A:HIS139 4.1 21.1 1.0
O A:PRO88 4.1 22.4 1.0
CG A:MET144 4.2 19.8 1.0
NE2 A:HIS89 4.2 20.5 1.0
CD2 A:HIS139 4.2 21.1 1.0
CD2 A:HIS89 4.3 20.0 1.0
CD A:PRO132 4.3 22.6 1.0
CA A:CYS130 4.6 18.7 1.0
SD A:MET56 4.6 24.9 1.0
CB A:MET144 4.7 17.7 1.0
N A:ASN90 4.7 20.0 1.0
CA A:HIS139 4.8 16.3 1.0
C A:HIS89 4.9 22.5 1.0
N A:HIS89 4.9 22.6 1.0
C A:PRO88 4.9 25.8 1.0

Copper binding site 2 out of 4 in 4csp

Go back to Copper Binding Sites List in 4csp
Copper binding site 2 out of 4 in the Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:17.3
occ:1.00
 O A:HOH2137 1.8 31.9 1.0
NE2 A:HIS129 2.1 15.9 1.0
NE2 A:HIS94 2.1 17.3 1.0
CE1 A:HIS94 2.9 17.6 1.0
CD2 A:HIS129 3.0 14.8 1.0
CE1 A:HIS129 3.1 15.8 1.0
CD2 A:HIS94 3.2 15.6 1.0
OD2 A:ASP92 3.7 29.1 1.0
ND1 A:HIS94 4.1 16.7 1.0
O A:HOH2057 4.1 42.2 1.0
CG A:HIS129 4.1 14.9 1.0
ND1 A:HIS129 4.2 14.8 1.0
CG A:HIS94 4.2 16.4 1.0
CG A:ASP92 4.3 25.5 1.0
OD1 A:ASP92 4.6 24.4 1.0

Copper binding site 3 out of 4 in 4csp

Go back to Copper Binding Sites List in 4csp
Copper binding site 3 out of 4 in the Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu501

b:24.1
occ:1.00
 ND1 F:HIS139 2.0 20.2 1.0
SG F:CYS130 2.1 22.9 1.0
ND1 F:HIS89 2.2 23.3 1.0
SD F:MET144 2.6 24.1 1.0
CE1 F:HIS139 2.9 20.9 1.0
CE1 F:HIS89 3.0 26.5 1.0
CG F:HIS139 3.1 20.3 1.0
CB F:CYS130 3.1 22.2 1.0
CG F:HIS89 3.2 26.3 1.0
CE F:MET144 3.5 23.4 1.0
CB F:HIS139 3.5 19.0 1.0
CB F:HIS89 3.5 24.8 1.0
CA F:HIS89 3.8 24.2 1.0
CG F:PRO132 4.0 27.5 1.0
NE2 F:HIS139 4.1 21.5 1.0
CG F:MET144 4.1 20.6 1.0
CD2 F:HIS139 4.2 20.8 1.0
NE2 F:HIS89 4.2 26.7 1.0
O F:PRO88 4.2 24.8 1.0
CD2 F:HIS89 4.3 26.2 1.0
CD F:PRO132 4.3 26.2 1.0
SD F:MET56 4.4 25.8 1.0
CB F:MET144 4.5 19.5 1.0
CA F:CYS130 4.6 20.5 1.0
N F:ASN90 4.7 27.1 1.0
CA F:HIS139 4.7 16.6 1.0
C F:HIS89 4.8 26.1 1.0
N F:HIS89 4.9 27.2 1.0
C F:PRO88 4.9 27.1 1.0

Copper binding site 4 out of 4 in 4csp

Go back to Copper Binding Sites List in 4csp
Copper binding site 4 out of 4 in the Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Structure of the F306C Mutant of Nitrite Reductase From Achromobacter Xylosoxidans within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu502

b:18.4
occ:1.00
 O F:HOH2113 1.3 22.0 0.5
NE2 F:HIS129 2.0 18.9 1.0
NE2 F:HIS94 2.1 19.0 1.0
CD2 F:HIS129 3.0 16.9 1.0
CE1 F:HIS94 3.0 17.4 1.0
CE1 F:HIS129 3.0 17.9 1.0
CD2 F:HIS94 3.2 19.6 1.0
OD2 F:ASP92 3.7 28.0 1.0
O F:HOH2113 4.1 24.1 0.5
ND1 F:HIS129 4.1 16.6 1.0
CG F:HIS129 4.1 17.6 1.0
ND1 F:HIS94 4.2 18.2 1.0
CG F:HIS94 4.3 18.9 1.0
CG F:ASP92 4.4 26.3 1.0
OD1 F:ASP92 4.7 25.9 1.0

Reference:

N.G.H.Leferink, S.V.Antonyuk, J.A.Houwman, N.S.Scrutton, R.R.Eady, S.S.Hasnain. Impact of Residues Remote From the Catalytic Centre on Enzyme Catalysis of Copper Nitrite Reductase. Nat.Commun. V. 5 4395 2014.
ISSN: ISSN 2041-1723
PubMed: 25022223
DOI: 10.1038/NCOMMS5395
Page generated: Wed Jul 31 02:40:43 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy