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Atomistry » Vanadium » PDB 4zi4-6py9 » 6fea | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Vanadium » PDB 4zi4-6py9 » 6fea » |
Vanadium in PDB 6fea: A. Vinelandii Vanadium Nitrogenase, Turnover StateEnzymatic activity of A. Vinelandii Vanadium Nitrogenase, Turnover State
All present enzymatic activity of A. Vinelandii Vanadium Nitrogenase, Turnover State:
1.18.6.1; Protein crystallography data
The structure of A. Vinelandii Vanadium Nitrogenase, Turnover State, PDB code: 6fea
was solved by
D.Sippel,
O.Einsle,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6fea:
The structure of A. Vinelandii Vanadium Nitrogenase, Turnover State also contains other interesting chemical elements:
Vanadium Binding Sites:
The binding sites of Vanadium atom in the A. Vinelandii Vanadium Nitrogenase, Turnover State
(pdb code 6fea). This binding sites where shown within
5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the A. Vinelandii Vanadium Nitrogenase, Turnover State, PDB code: 6fea: Jump to Vanadium binding site number: 1; 2; Vanadium binding site 1 out of 2 in 6feaGo back to![]() ![]()
Vanadium binding site 1 out
of 2 in the A. Vinelandii Vanadium Nitrogenase, Turnover State
![]() Mono view ![]() Stereo pair view
Vanadium binding site 2 out of 2 in 6feaGo back to![]() ![]()
Vanadium binding site 2 out
of 2 in the A. Vinelandii Vanadium Nitrogenase, Turnover State
![]() Mono view ![]() Stereo pair view
Reference:
D.Sippel,
M.Rohde,
J.Netzer,
C.Trncik,
J.Gies,
K.Grunau,
I.Djurdjevic,
L.Decamps,
S.L.A.Andrade,
O.Einsle.
A Bound Reaction Intermediate Sheds Light on the Mechanism of Nitrogenase. Science V. 359 1484 2018.
Page generated: Wed Dec 16 02:31:45 2020
ISSN: ESSN 1095-9203 PubMed: 29599235 DOI: 10.1126/SCIENCE.AAR2765 |
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