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Atomistry » Zinc » PDB 2aqq-2b63 » 2b0z | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2aqq-2b63 » 2b0z » |
Zinc in PDB 2b0z: Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C PeroxidaseEnzymatic activity of Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase
All present enzymatic activity of Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase:
1.11.1.5; Protein crystallography data
The structure of Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b0z
was solved by
S.A.Kang,
B.R.Crane,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2b0z:
The structure of Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase
(pdb code 2b0z). 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 Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase, PDB code: 2b0z: Zinc binding site 1 out of 1 in 2b0zGo back to Zinc Binding Sites List in 2b0z
Zinc binding site 1 out
of 1 in the Crystal Structure of the Protein-Protein Complex Between F82I Cytochrome C and Cytochrome C Peroxidase
Mono view Stereo pair view
Reference:
S.A.Kang,
B.R.Crane.
Effects of Interface Mutations on Association Modes and Electron-Transfer Rates Between Proteins Proc.Natl.Acad.Sci.Usa V. 102 15465 2005.
Page generated: Wed Dec 16 03:18:00 2020
ISSN: ISSN 0027-8424 PubMed: 16227441 DOI: 10.1073/PNAS.0505176102 |
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