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Atomistry » Iron » PDB 2yeq-2z4g » 2yvj | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 2yeq-2z4g » 2yvj » |
Iron in PDB 2yvj: Crystal Structure of the Ferredoxin-Ferredoxin Reductase (BPHA3-BPHA4)ComplexEnzymatic activity of Crystal Structure of the Ferredoxin-Ferredoxin Reductase (BPHA3-BPHA4)Complex
All present enzymatic activity of Crystal Structure of the Ferredoxin-Ferredoxin Reductase (BPHA3-BPHA4)Complex:
1.18.1.2; Protein crystallography data
The structure of Crystal Structure of the Ferredoxin-Ferredoxin Reductase (BPHA3-BPHA4)Complex, PDB code: 2yvj
was solved by
T.Senda,
M.Senda,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of the Ferredoxin-Ferredoxin Reductase (BPHA3-BPHA4)Complex
(pdb code 2yvj). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of the Ferredoxin-Ferredoxin Reductase (BPHA3-BPHA4)Complex, PDB code: 2yvj: Jump to Iron binding site number: 1; 2; Iron binding site 1 out of 2 in 2yvjGo back to Iron Binding Sites List in 2yvj
Iron binding site 1 out
of 2 in the Crystal Structure of the Ferredoxin-Ferredoxin Reductase (BPHA3-BPHA4)Complex
Mono view Stereo pair view
Iron binding site 2 out of 2 in 2yvjGo back to Iron Binding Sites List in 2yvj
Iron binding site 2 out
of 2 in the Crystal Structure of the Ferredoxin-Ferredoxin Reductase (BPHA3-BPHA4)Complex
Mono view Stereo pair view
Reference:
M.Senda,
S.Kishigami,
S.Kimura,
M.Fukuda,
T.Ishida,
T.Senda.
Molecular Mechanism of the Redox-Dependent Interaction Between Nadh-Dependent Ferredoxin Reductase and Rieske-Type [2FE-2S] Ferredoxin J.Mol.Biol. V. 373 382 2007.
Page generated: Sun Aug 4 05:45:09 2024
ISSN: ISSN 0022-2836 PubMed: 17850818 DOI: 10.1016/J.JMB.2007.08.002 |
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