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Atomistry » Zinc » PDB 3m1k-3m6o » 3m2v | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3m1k-3m6o » 3m2v » |
Zinc in PDB 3m2v: Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B AnaloguesEnzymatic activity of Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues
All present enzymatic activity of Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues:
2.8.4.1; Protein crystallography data
The structure of Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues, PDB code: 3m2v
was solved by
P.E.Cedervall,
M.Dey,
S.W.Ragsdale,
C.M.Wilmot,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3m2v:
The structure of Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues
(pdb code 3m2v). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues, PDB code: 3m2v: Zinc binding site 1 out of 1 in 3m2vGo back to Zinc Binding Sites List in 3m2v
Zinc binding site 1 out
of 1 in the Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues
Mono view Stereo pair view
Reference:
P.E.Cedervall,
M.Dey,
A.R.Pearson,
S.W.Ragsdale,
C.M.Wilmot.
Structural Insight Into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues. Biochemistry V. 49 7683 2010.
Page generated: Wed Dec 16 04:33:50 2020
ISSN: ISSN 0006-2960 PubMed: 20707311 DOI: 10.1021/BI100458D |
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