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Copper in PDB 2vm4: Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2

Protein crystallography data

The structure of Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2, PDB code: 2vm4 was solved by M.A.Hough, S.V.Antonyuk, R.W.Strange, 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) 68.68 / 1.90
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 90.143, 90.143, 143.753, 90.00, 90.00, 120.00
R / Rfree (%) 17.8 / 21.4

Other elements in 2vm4:

The structure of Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2 also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2 (pdb code 2vm4). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2, PDB code: 2vm4:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2vm4

Go back to Copper Binding Sites List in 2vm4
Copper binding site 1 out of 2 in the Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:21.7
occ:1.00
ND1 A:HIS139 2.1 17.4 1.0
SG A:CYS130 2.2 18.8 1.0
ND1 A:HIS89 2.2 18.9 1.0
SD A:MET144 2.5 18.8 1.0
CE1 A:HIS139 3.1 18.3 1.0
CB A:CYS130 3.1 18.3 1.0
CG A:HIS139 3.1 16.7 1.0
CE1 A:HIS89 3.2 20.5 1.0
CG A:HIS89 3.2 20.6 1.0
CB A:HIS89 3.5 20.9 1.0
CB A:HIS139 3.5 14.3 1.0
CE A:MET144 3.5 17.1 1.0
CA A:HIS89 3.9 21.2 1.0
CG A:PRO132 4.0 21.1 1.0
CG A:MET144 4.1 18.1 1.0
O A:PRO88 4.1 20.9 1.0
NE2 A:HIS139 4.2 19.6 1.0
CD2 A:HIS139 4.3 16.5 1.0
NE2 A:HIS89 4.3 20.5 1.0
CD A:PRO132 4.3 20.0 1.0
CD2 A:HIS89 4.4 21.2 1.0
SD A:MET56 4.4 20.9 1.0
CA A:CYS130 4.5 17.6 1.0
CB A:MET144 4.6 15.9 1.0
CA A:HIS139 4.7 14.2 1.0
N A:ASN90 4.7 20.4 1.0
N A:HIS89 4.8 21.8 1.0
C A:PRO88 4.9 22.5 1.0
C A:HIS89 4.9 21.5 1.0
C A:CYS130 5.0 18.5 1.0

Copper binding site 2 out of 2 in 2vm4

Go back to Copper Binding Sites List in 2vm4
Copper binding site 2 out of 2 in the Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Alcaligenes Xylosoxidans Nitrite Reductase in Space Group R3 - 2 of 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:15.9
occ:1.00
O A:HOH2065 1.9 19.7 1.0
NE2 A:HIS129 1.9 14.9 1.0
NE2 A:HIS94 2.0 17.6 1.0
CE1 A:HIS94 2.9 14.7 1.0
CD2 A:HIS129 2.9 12.4 1.0
CE1 A:HIS129 2.9 16.1 1.0
CD2 A:HIS94 3.1 14.5 1.0
OD2 A:ASP92 3.5 27.8 1.0
ND1 A:HIS129 4.0 14.3 1.0
CG A:HIS129 4.1 16.1 1.0
ND1 A:HIS94 4.1 17.6 1.0
CG A:HIS94 4.2 16.1 1.0
CG A:ASP92 4.2 23.6 1.0
OD1 A:ASP92 4.5 23.0 1.0

Reference:

M.A.Hough, S.V.Antonyuk, R.W.Strange, R.R.Eady, S.S.Hasnain. Crystallography with Online Optical and X-Ray Absorption Spectroscopies Demonstrates An Ordered Mechanism in Copper Nitrite Reductase. J.Mol.Biol. V. 378 353 2008.
ISSN: ISSN 0022-2836
PubMed: 18353369
DOI: 10.1016/J.JMB.2008.01.097
Page generated: Sun Dec 13 11:07:09 2020

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