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Cobalt in PDB 9fvs: Crystal Structure of Heme-Oxygenase Mutant G139A From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III))Enzymatic activity of Crystal Structure of Heme-Oxygenase Mutant G139A From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III))
All present enzymatic activity of Crystal Structure of Heme-Oxygenase Mutant G139A From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)):
1.14.14.18; Protein crystallography data
The structure of Crystal Structure of Heme-Oxygenase Mutant G139A From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)), PDB code: 9fvs
was solved by
R.J.Labidi,
B.Faivre,
P.Carpentier,
J.Perard,
P.Gotico,
Y.Li,
M.Atta,
M.Fontecave,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 9fvs:
The structure of Crystal Structure of Heme-Oxygenase Mutant G139A From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)) also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Crystal Structure of Heme-Oxygenase Mutant G139A From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III))
(pdb code 9fvs). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of Heme-Oxygenase Mutant G139A From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III)), PDB code: 9fvs: Cobalt binding site 1 out of 1 in 9fvsGo back to Cobalt Binding Sites List in 9fvs
Cobalt binding site 1 out
of 1 in the Crystal Structure of Heme-Oxygenase Mutant G139A From Corynebacterium Diphtheriae Complexed with Cobalt-Porphyrine (Humo-Co(III))
Mono view Stereo pair view
Reference:
R.J.Labidi,
B.Faivre,
P.Carpentier,
J.Perard,
P.Gotico,
Y.Li,
M.Atta,
M.Fontecave.
Light-Activated Artificial Co 2 -Reductase: Structure and Activity. J.Am.Chem.Soc. 2024.
Page generated: Thu Oct 31 18:19:57 2024
ISSN: ESSN 1520-5126 PubMed: 39352411 DOI: 10.1021/JACS.4C08927 |
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