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Zinc in PDB 2vw4: Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3

Enzymatic activity of Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3

All present enzymatic activity of Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3:
1.7.2.1;

Protein crystallography data

The structure of Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3, PDB code: 2vw4 was solved by M.J.Ellis, S.G.Buffey, M.A.Hough, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 96.23 / 1.90
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 89.080, 89.080, 288.303, 90.00, 90.00, 120.00
R / Rfree (%) 16.2 / 19.7

Other elements in 2vw4:

The structure of Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3 also contains other interesting chemical elements:

Copper (Cu) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3 (pdb code 2vw4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3, PDB code: 2vw4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2vw4

Go back to Zinc Binding Sites List in 2vw4
Zinc binding site 1 out of 2 in the Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn503

b:25.2
occ:1.00
NE2 B:HIS165 2.0 15.5 1.0
OE2 A:GLU195 2.0 16.9 0.5
OD2 B:ASP167 2.1 18.6 1.0
OE1 A:GLU195 2.3 17.3 0.5
OD1 B:ASP167 2.5 20.5 1.0
CG B:ASP167 2.6 19.0 1.0
OE2 A:GLU195 2.7 17.7 0.5
CD A:GLU195 2.8 17.2 1.0
OE1 A:GLU195 2.9 15.9 0.5
CE1 B:HIS165 2.9 17.5 1.0
CD2 B:HIS165 3.0 16.7 1.0
O A:HOH2239 3.6 34.8 1.0
ND1 B:HIS165 4.0 17.0 1.0
OG1 B:THR234 4.1 19.9 1.0
CB B:ASP167 4.1 19.6 1.0
O A:HOH2243 4.1 26.2 1.0
CG B:HIS165 4.1 16.9 1.0
CG A:GLU195 4.2 18.3 1.0
CB B:THR234 4.3 20.7 1.0
O B:HOH2243 4.4 27.9 1.0
N B:THR234 4.5 20.6 1.0
N B:ASP167 4.6 18.5 1.0
CB A:ALA191 4.6 18.2 1.0
O B:GLY232 4.8 22.9 1.0
CA B:ASP167 4.8 19.0 1.0

Zinc binding site 2 out of 2 in 2vw4

Go back to Zinc Binding Sites List in 2vw4
Zinc binding site 2 out of 2 in the Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Nitrite Reductase From Alcaligenes Xylosoxidans - 2 of 3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn503

b:23.3
occ:1.00
NE2 A:HIS165 1.9 15.2 1.0
OD2 A:ASP167 2.1 16.9 1.0
OD1 A:ASP167 2.4 18.1 1.0
CG A:ASP167 2.6 17.5 1.0
CD2 A:HIS165 2.9 16.4 1.0
CE1 A:HIS165 2.9 15.4 1.0
OG1 A:THR234 4.0 15.8 1.0
ND1 A:HIS165 4.0 15.9 1.0
CG A:HIS165 4.0 16.0 1.0
CB A:ASP167 4.1 17.5 1.0
O A:HOH2273 4.1 23.4 1.0
CB A:THR234 4.3 16.1 1.0
N A:THR234 4.5 17.5 1.0
N A:ASP167 4.6 16.5 1.0
CA A:ASP167 4.8 17.4 1.0
O A:GLY232 4.8 20.3 1.0
C A:TYR166 5.0 15.4 1.0

Reference:

M.J.Ellis, S.G.Buffey, M.A.Hough, S.S.Hasnain. On-Line Optical and X-Ray Spectroscopies with Crystallography: An Integrated Approach For Determining Metalloprotein Structures in Functionally Well Defined States. J.Synchrotron Radiat. V. 15 433 2008.
ISSN: ISSN 0909-0495
PubMed: 18728313
DOI: 10.1107/S0909049508014945
Page generated: Wed Aug 20 06:14:01 2025

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