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Atomistry » Mercury » PDB 12ca-1czm » 1bic » |
Mercury in PDB 1bic: Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-Enzymatic activity of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-
All present enzymatic activity of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-:
4.2.1.1; Protein crystallography data
The structure of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-, PDB code: 1bic
was solved by
Y.Xue,
J.Vidgren,
L.A.Svensson,
A.Liljas,
B.-H.Jonsson,
S.Lindskog,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1bic:
The structure of Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3- also contains other interesting chemical elements:
Mercury Binding Sites:
The binding sites of Mercury atom in the Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-
(pdb code 1bic). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-, PDB code: 1bic: Mercury binding site 1 out of 1 in 1bicGo back to![]() ![]()
Mercury binding site 1 out
of 1 in the Crystallographic Analysis of Thr-200-> His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-
![]() Mono view ![]() Stereo pair view
Reference:
Y.Xue,
J.Vidgren,
L.A.Svensson,
A.Liljas,
B.H.Jonsson,
S.Lindskog.
Crystallographic Analysis of Thr-200-->His Human Carbonic Anhydrase II and Its Complex with the Substrate, HCO3-. Proteins V. 15 80 1993.
Page generated: Sat Aug 10 23:19:17 2024
ISSN: ISSN 0887-3585 PubMed: 8451242 DOI: 10.1002/PROT.340150110 |
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