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Atomistry » Chlorine » PDB 6q91-6qie » 6qfw » |
Chlorine in PDB 6qfw: Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 9) to Generate An Artificial Transfer Hydrogenase (Athase)Enzymatic activity of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 9) to Generate An Artificial Transfer Hydrogenase (Athase)
All present enzymatic activity of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 9) to Generate An Artificial Transfer Hydrogenase (Athase):
4.2.1.1; Protein crystallography data
The structure of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 9) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfw
was solved by
J.G.Rebelein,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6qfw:
The structure of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 9) to Generate An Artificial Transfer Hydrogenase (Athase) also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 9) to Generate An Artificial Transfer Hydrogenase (Athase)
(pdb code 6qfw). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 9) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfw: Chlorine binding site 1 out of 1 in 6qfwGo back to Chlorine Binding Sites List in 6qfw
Chlorine binding site 1 out
of 1 in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 9) to Generate An Artificial Transfer Hydrogenase (Athase)
Mono view Stereo pair view
Reference:
J.G.Rebelein,
Y.Cotelle,
B.Garabedian,
T.R.Ward.
Chemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase As Host Protein. Acs Catalysis V. 9 4173 2019.
Page generated: Mon Jul 29 13:56:34 2024
ISSN: ESSN 2155-5435 PubMed: 31080690 DOI: 10.1021/ACSCATAL.9B01006 |
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