Atomistry » Copper » PDB 2xv2-2z7w » 2xxf
Atomistry »
  Copper »
    PDB 2xv2-2z7w »
      2xxf »

Copper in PDB 2xxf: Cu Metallated H254F Mutant of Nitrite Reductase

Protein crystallography data

The structure of Cu Metallated H254F Mutant of Nitrite Reductase, PDB code: 2xxf was solved by M.A.Hough, R.R.Eady, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 95.78 / 1.50
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 89.333, 89.333, 287.851, 90.00, 90.00, 120.00
R / Rfree (%) 14.462 / 17.65

Other elements in 2xxf:

The structure of Cu Metallated H254F Mutant of Nitrite Reductase also contains other interesting chemical elements:

Zinc (Zn) 6 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Cu Metallated H254F Mutant of Nitrite Reductase (pdb code 2xxf). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Cu Metallated H254F Mutant of Nitrite Reductase, PDB code: 2xxf:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 2xxf

Go back to Copper Binding Sites List in 2xxf
Copper binding site 1 out of 4 in the Cu Metallated H254F Mutant of Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu Metallated H254F Mutant of Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1337

b:25.3
occ:1.00
ND1 A:HIS89 2.0 24.2 1.0
ND1 A:HIS139 2.0 22.4 1.0
SG A:CYS130 2.1 24.5 1.0
SD A:MET144 2.6 24.9 1.0
CE1 A:HIS89 2.9 24.3 1.0
CE1 A:HIS139 3.0 22.7 1.0
CG A:HIS89 3.1 25.1 1.0
CG A:HIS139 3.1 21.1 1.0
CB A:CYS130 3.2 20.8 1.0
CB A:HIS89 3.5 23.7 1.0
CB A:HIS139 3.5 18.8 1.0
CE A:MET144 3.5 25.0 1.0
CA A:HIS89 3.8 24.6 1.0
CG A:PRO132 3.9 23.8 1.0
O A:PRO88 4.1 25.6 1.0
NE2 A:HIS89 4.1 26.6 1.0
CG A:MET144 4.1 21.7 1.0
NE2 A:HIS139 4.1 22.1 1.0
CD2 A:HIS89 4.2 25.0 1.0
CD2 A:HIS139 4.2 20.8 1.0
CD A:PRO132 4.3 22.7 1.0
SD A:MET56 4.4 26.1 1.0
CB A:MET144 4.6 19.2 1.0
CA A:CYS130 4.6 20.1 1.0
CA A:HIS139 4.7 18.4 1.0
N A:ASN90 4.7 24.2 1.0
N A:HIS89 4.8 25.7 1.0
C A:PRO88 4.8 27.3 1.0
C A:HIS89 4.8 23.7 1.0

Copper binding site 2 out of 4 in 2xxf

Go back to Copper Binding Sites List in 2xxf
Copper binding site 2 out of 4 in the Cu Metallated H254F Mutant of Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu Metallated H254F Mutant of Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1338

b:14.6
occ:0.30
ZN A:ZN1339 0.6 15.8 0.7
O A:HOH2281 1.7 22.8 1.0
NE2 A:HIS94 2.0 16.6 1.0
NE2 A:HIS129 2.4 18.0 1.0
CE1 A:HIS94 3.0 17.9 1.0
CD2 A:HIS94 3.0 18.0 1.0
CE1 A:HIS129 3.4 20.2 1.0
CD2 A:HIS129 3.4 16.5 1.0
OD2 A:ASP92 3.5 26.7 1.0
ND1 A:HIS94 4.1 17.0 1.0
CG A:HIS94 4.1 18.0 1.0
CG A:ASP92 4.2 23.5 1.0
OD1 A:ASP92 4.4 25.4 1.0
ND1 A:HIS129 4.5 19.1 1.0
CG A:HIS129 4.6 18.1 1.0
O A:HOH2101 4.7 31.0 1.0

Copper binding site 3 out of 4 in 2xxf

Go back to Copper Binding Sites List in 2xxf
Copper binding site 3 out of 4 in the Cu Metallated H254F Mutant of Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Cu Metallated H254F Mutant of Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1337

b:23.8
occ:1.00
ND1 B:HIS89 2.1 21.6 1.0
ND1 B:HIS139 2.1 21.3 1.0
SG B:CYS130 2.2 21.2 1.0
SD B:MET144 2.6 22.3 1.0
CE1 B:HIS139 3.0 23.6 1.0
CE1 B:HIS89 3.0 23.4 1.0
CG B:HIS139 3.1 18.5 1.0
CG B:HIS89 3.1 23.0 1.0
CB B:CYS130 3.2 18.2 1.0
CB B:HIS89 3.5 22.4 1.0
CB B:HIS139 3.5 18.7 1.0
CE B:MET144 3.6 23.9 1.0
CA B:HIS89 3.8 22.8 1.0
CG B:PRO132 4.0 21.4 1.0
O B:PRO88 4.1 26.4 1.0
NE2 B:HIS139 4.1 21.2 1.0
CG B:MET144 4.1 18.3 1.0
NE2 B:HIS89 4.2 23.5 1.0
CD2 B:HIS139 4.2 19.5 1.0
CD2 B:HIS89 4.2 23.4 1.0
CD B:PRO132 4.3 20.5 1.0
SD B:MET56 4.4 23.2 1.0
CA B:CYS130 4.6 18.5 1.0
CB B:MET144 4.7 17.9 1.0
CA B:HIS139 4.7 16.8 1.0
N B:ASN90 4.7 21.7 1.0
N B:HIS89 4.8 24.4 1.0
C B:PRO88 4.8 26.2 1.0
C B:HIS89 4.8 23.1 1.0

Copper binding site 4 out of 4 in 2xxf

Go back to Copper Binding Sites List in 2xxf
Copper binding site 4 out of 4 in the Cu Metallated H254F Mutant of Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Cu Metallated H254F Mutant of Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1340

b:10.5
occ:0.30
ZN B:ZN1338 0.4 18.6 0.7
O B:HOH2308 1.8 19.0 1.0
NE2 B:HIS94 1.9 15.3 1.0
NE2 B:HIS129 2.2 15.0 1.0
CE1 B:HIS94 2.9 15.9 1.0
CD2 B:HIS94 3.0 15.4 1.0
CD2 B:HIS129 3.1 16.3 1.0
CE1 B:HIS129 3.2 16.9 1.0
OD2 B:ASP92 3.6 22.2 1.0
ND1 B:HIS94 4.0 15.8 1.0
CG B:HIS94 4.1 16.3 1.0
CG B:ASP92 4.1 24.2 1.0
CG B:HIS129 4.3 15.5 1.0
ND1 B:HIS129 4.3 16.8 1.0
OD1 B:ASP92 4.4 24.9 1.0
O B:HOH2111 4.9 26.3 1.0

Reference:

N.G.H.Leferink, C.Han, S.V.Antonyuk, D.J.Heyes, S.E.J.Rigby, M.A.Hough, R.R.Eady, N.S.Scrutton, S.S.Hasnain. Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes Xylosoxidans Copper-Dependent Nitrite Reductase. Biochemistry V. 50 4121 2011.
ISSN: ISSN 0006-2960
PubMed: 21469743
DOI: 10.1021/BI200246F
Page generated: Sun Dec 13 11:07:48 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy