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Atomistry » Zinc » PDB 2bn7-2c6n » 2bno | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2bn7-2c6n » 2bno » |
Zinc in PDB 2bno: The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.Protein crystallography data
The structure of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis., PDB code: 2bno
was solved by
K.Mcluskey,
S.Cameron,
W.N.Hunter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2bno:
The structure of The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.
(pdb code 2bno). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis., PDB code: 2bno: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2bnoGo back to Zinc Binding Sites List in 2bno
Zinc binding site 1 out
of 2 in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2bnoGo back to Zinc Binding Sites List in 2bno
Zinc binding site 2 out
of 2 in the The Structure of Hydroxypropylphosphonic Acid Epoxidase From S. Wedmorenis.
Mono view Stereo pair view
Reference:
K.Mcluskey,
S.Cameron,
F.Hammerschmidt,
W.N.Hunter.
Structure and Reactivity of Hydroxypropylphosphonic Acid Epoxidase in Fosfomycin Biosynthesis By A Cation- and Flavin-Dependent Mechanism. Proc.Natl.Acad.Sci.Usa V. 102 14221 2005.
Page generated: Wed Dec 16 03:18:35 2020
ISSN: ISSN 0027-8424 PubMed: 16186494 DOI: 10.1073/PNAS.0504314102 |
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