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Atomistry » Zinc » PDB 2vqx-2w13 » 2vw6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2vqx-2w13 » 2vw6 » |
Zinc in PDB 2vw6: Nitrite Reductase From Alcaligenes Xylosoxidans - 3 of 3Enzymatic activity of Nitrite Reductase From Alcaligenes Xylosoxidans - 3 of 3
All present enzymatic activity of Nitrite Reductase From Alcaligenes Xylosoxidans - 3 of 3:
1.7.2.1; Protein crystallography data
The structure of Nitrite Reductase From Alcaligenes Xylosoxidans - 3 of 3, PDB code: 2vw6
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:
Other elements in 2vw6:
The structure of Nitrite Reductase From Alcaligenes Xylosoxidans - 3 of 3 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Nitrite Reductase From Alcaligenes Xylosoxidans - 3 of 3
(pdb code 2vw6). 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 - 3 of 3, PDB code: 2vw6: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2vw6Go back to Zinc Binding Sites List in 2vw6
Zinc binding site 1 out
of 2 in the Nitrite Reductase From Alcaligenes Xylosoxidans - 3 of 3
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2vw6Go back to Zinc Binding Sites List in 2vw6
Zinc binding site 2 out
of 2 in the Nitrite Reductase From Alcaligenes Xylosoxidans - 3 of 3
Mono view Stereo pair view
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.
Page generated: Thu Oct 17 04:38:10 2024
ISSN: ISSN 0909-0495 PubMed: 18728313 DOI: 10.1107/S0909049508014945 |
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