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Zinc in PDB 2vm3: Structure of Alcaligenes Xylosoxidans in Space Group R3 - 1 of 2

Protein crystallography data

The structure of Structure of Alcaligenes Xylosoxidans in Space Group R3 - 1 of 2, PDB code: 2vm3 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) 68.52 / 1.80
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 89.941, 89.941, 143.732, 90.00, 90.00, 120.00
R / Rfree (%) 18.4 / 21

Other elements in 2vm3:

The structure of Structure of Alcaligenes Xylosoxidans in Space Group R3 - 1 of 2 also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Alcaligenes Xylosoxidans in Space Group R3 - 1 of 2 (pdb code 2vm3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Alcaligenes Xylosoxidans in Space Group R3 - 1 of 2, PDB code: 2vm3:

Zinc binding site 1 out of 1 in 2vm3

Go back to Zinc Binding Sites List in 2vm3
Zinc binding site 1 out of 1 in the Structure of Alcaligenes Xylosoxidans in Space Group R3 - 1 of 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Alcaligenes Xylosoxidans in Space Group R3 - 1 of 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn888

b:26.5
occ:1.00
O A:HOH2229 1.7 20.4 1.0
NE2 A:HIS165 1.9 24.1 1.0
OD2 A:ASP167 2.1 26.2 1.0
OD1 A:ASP167 2.4 26.3 1.0
CG A:ASP167 2.6 25.0 1.0
CE1 A:HIS165 2.9 22.0 1.0
CD2 A:HIS165 3.0 23.5 1.0
O A:HOH2177 3.6 33.0 1.0
OG1 A:THR234 3.9 23.6 1.0
ND1 A:HIS165 4.0 22.7 1.0
CB A:ASP167 4.1 24.5 1.0
CG A:HIS165 4.1 22.1 1.0
CB A:THR234 4.3 24.1 1.0
N A:THR234 4.5 24.4 1.0
N A:ASP167 4.6 23.4 1.0
O A:GLY232 4.7 27.9 1.0
CA A:ASP167 4.8 24.7 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: Thu Oct 17 04:22:29 2024

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