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Zinc in PDB 7onv: Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase)Enzymatic activity of Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase)
All present enzymatic activity of Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase):
4.2.1.1; 4.2.1.69; Protein crystallography data
The structure of Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 7onv
was solved by
A.Stein,
C.Dongping,
Y.Cotelle,
J.G.Rebelein,
T.R.Ward,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7onv:
The structure of Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase) also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase)
(pdb code 7onv). 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 Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 7onv: Zinc binding site 1 out of 1 in 7onvGo back to Zinc Binding Sites List in 7onv
Zinc binding site 1 out
of 1 in the Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase)
Mono view Stereo pair view
Reference:
A.Stein,
D.Chen,
N.V.Igareta,
Y.Cotelle,
J.G.Rebelein,
T.R.Ward.
A Dual Anchoring Strategy For the Directed Evolution of Improved Artificial Transfer Hydrogenases Based on Carbonic Anhydrase. Acs Cent.Sci. V. 7 1874 2021.
Page generated: Sat Apr 8 01:10:48 2023
ISSN: ESSN 2374-7951 PubMed: 34849402 DOI: 10.1021/ACSCENTSCI.1C00825 |
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