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Atomistry » Zinc » PDB 4h8p-4hk6 » 4hba » |
Zinc in PDB 4hba: Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide BondEnzymatic activity of Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond
All present enzymatic activity of Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond:
4.2.1.1; Protein crystallography data
The structure of Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond, PDB code: 4hba
was solved by
C.D.Boone,
A.Habibzadegan,
R.Mckenna,
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 Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond
(pdb code 4hba). 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 Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond, PDB code: 4hba: Zinc binding site 1 out of 1 in 4hbaGo back to Zinc Binding Sites List in 4hba
Zinc binding site 1 out
of 1 in the Structural and Catalytic Characterization of A Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond
Mono view Stereo pair view
Reference:
C.D.Boone,
A.Habibzadegan,
C.Tu,
D.N.Silverman,
R.Mckenna.
Structural and Catalytic Characterization of A Thermally Stable and Acid-Stable Variant of Human Carbonic Anhydrase II Containing An Engineered Disulfide Bond. Acta Crystallogr.,Sect.D V. 69 1414 2013.
Page generated: Wed Dec 16 05:21:56 2020
ISSN: ISSN 0907-4449 PubMed: 23897465 DOI: 10.1107/S0907444913008743 |
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