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Atomistry » Zinc » PDB 1v0d-1vdd » 1v13 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1v0d-1vdd » 1v13 » |
Zinc in PDB 1v13: Crystal Structure of the Mutant HIS103ALA of the Colicin E9 Dnase Domain in Complex with Zn+2 (2.0 Angstroms)Protein crystallography data
The structure of Crystal Structure of the Mutant HIS103ALA of the Colicin E9 Dnase Domain in Complex with Zn+2 (2.0 Angstroms), PDB code: 1v13
was solved by
M.J.Mate,
C.Kleanthous,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Mutant HIS103ALA of the Colicin E9 Dnase Domain in Complex with Zn+2 (2.0 Angstroms)
(pdb code 1v13). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Mutant HIS103ALA of the Colicin E9 Dnase Domain in Complex with Zn+2 (2.0 Angstroms), PDB code: 1v13: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 1v13Go back to Zinc Binding Sites List in 1v13
Zinc binding site 1 out
of 2 in the Crystal Structure of the Mutant HIS103ALA of the Colicin E9 Dnase Domain in Complex with Zn+2 (2.0 Angstroms)
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 1v13Go back to Zinc Binding Sites List in 1v13
Zinc binding site 2 out
of 2 in the Crystal Structure of the Mutant HIS103ALA of the Colicin E9 Dnase Domain in Complex with Zn+2 (2.0 Angstroms)
Mono view Stereo pair view
Reference:
M.J.Mate,
C.Kleanthous.
Structure-Based Analysis of the Metal-Dependent Mechanism of H-N-H Endonucleases J.Biol.Chem. V. 279 34763 2004.
Page generated: Wed Oct 16 19:41:54 2024
ISSN: ISSN 0021-9258 PubMed: 15190054 DOI: 10.1074/JBC.M403719200 |
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