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Zinc in PDB 6cpa: Crystal Structure of the Complex of Carboxypeptidase A with A Strongly Bound Phosphonate in A New Crystalline Form: Comparison with Structures of Other ComplexesEnzymatic activity of Crystal Structure of the Complex of Carboxypeptidase A with A Strongly Bound Phosphonate in A New Crystalline Form: Comparison with Structures of Other Complexes
All present enzymatic activity of Crystal Structure of the Complex of Carboxypeptidase A with A Strongly Bound Phosphonate in A New Crystalline Form: Comparison with Structures of Other Complexes:
3.4.17.1; Protein crystallography data
The structure of Crystal Structure of the Complex of Carboxypeptidase A with A Strongly Bound Phosphonate in A New Crystalline Form: Comparison with Structures of Other Complexes, PDB code: 6cpa
was solved by
H.Kim,
W.N.Lipscomb,
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 Complex of Carboxypeptidase A with A Strongly Bound Phosphonate in A New Crystalline Form: Comparison with Structures of Other Complexes
(pdb code 6cpa). 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 Complex of Carboxypeptidase A with A Strongly Bound Phosphonate in A New Crystalline Form: Comparison with Structures of Other Complexes, PDB code: 6cpa: Zinc binding site 1 out of 1 in 6cpaGo back to Zinc Binding Sites List in 6cpa
Zinc binding site 1 out
of 1 in the Crystal Structure of the Complex of Carboxypeptidase A with A Strongly Bound Phosphonate in A New Crystalline Form: Comparison with Structures of Other Complexes
Mono view Stereo pair view
Reference:
H.Kim,
W.N.Lipscomb.
Crystal Structure of the Complex of Carboxypeptidase A with A Strongly Bound Phosphonate in A New Crystalline Form: Comparison with Structures of Other Complexes. Biochemistry V. 29 5546 1990.
Page generated: Wed Dec 16 11:37:30 2020
ISSN: ISSN 0006-2960 PubMed: 2386784 DOI: 10.1021/BI00475A019 |
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