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Atomistry » Zinc » PDB 1z3j-1zfk » 1z8j » |
Zinc in PDB 1z8j: Crystal Structure of the Thrombin Mutant G193P Bound to PpackEnzymatic activity of Crystal Structure of the Thrombin Mutant G193P Bound to Ppack
All present enzymatic activity of Crystal Structure of the Thrombin Mutant G193P Bound to Ppack:
3.4.21.5; Protein crystallography data
The structure of Crystal Structure of the Thrombin Mutant G193P Bound to Ppack, PDB code: 1z8j
was solved by
K.M.Bobofchak,
A.O.Pineda,
F.S.Mathews,
E.Di Cera,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1z8j:
The structure of Crystal Structure of the Thrombin Mutant G193P Bound to Ppack also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Thrombin Mutant G193P Bound to Ppack
(pdb code 1z8j). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of the Thrombin Mutant G193P Bound to Ppack, PDB code: 1z8j: Jump to Zinc binding site number: 1; 2; 3; Zinc binding site 1 out of 3 in 1z8jGo back to Zinc Binding Sites List in 1z8j
Zinc binding site 1 out
of 3 in the Crystal Structure of the Thrombin Mutant G193P Bound to Ppack
Mono view Stereo pair view
Zinc binding site 2 out of 3 in 1z8jGo back to Zinc Binding Sites List in 1z8j
Zinc binding site 2 out
of 3 in the Crystal Structure of the Thrombin Mutant G193P Bound to Ppack
Mono view Stereo pair view
Zinc binding site 3 out of 3 in 1z8jGo back to Zinc Binding Sites List in 1z8j
Zinc binding site 3 out
of 3 in the Crystal Structure of the Thrombin Mutant G193P Bound to Ppack
Mono view Stereo pair view
Reference:
K.M.Bobofchak,
A.O.Pineda,
F.S.Mathews,
E.Di Cera.
Energetic and Structural Consequences of Perturbing Gly-193 in the Oxyanion Hole of Serine Proteases J.Biol.Chem. V. 280 25644 2005.
Page generated: Wed Dec 16 03:15:24 2020
ISSN: ISSN 0021-9258 PubMed: 15890651 DOI: 10.1074/JBC.M503499200 |
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