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Zinc in PDB 4ar9: Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.Enzymatic activity of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.
All present enzymatic activity of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.:
3.4.24.3; Protein crystallography data
The structure of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution., PDB code: 4ar9
was solved by
U.Eckhard,
H.Brandstetter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4ar9:
The structure of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.
(pdb code 4ar9). 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 Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution., PDB code: 4ar9: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 4ar9Go back to Zinc Binding Sites List in 4ar9
Zinc binding site 1 out
of 2 in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 4ar9Go back to Zinc Binding Sites List in 4ar9
Zinc binding site 2 out
of 2 in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.
Mono view Stereo pair view
Reference:
U.Eckhard,
E.Schonauer,
H.Brandstetter.
Structural Basis For Activity Regulation and Substrate Preference of Clostridial Collagenases G, H, and T. J.Biol.Chem. V. 288 20184 2013.
Page generated: Wed Dec 16 05:03:39 2020
ISSN: ISSN 0021-9258 PubMed: 23703618 DOI: 10.1074/JBC.M112.448548 |
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