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Zinc in PDB 8dpc: Crystal Structure of Carbonic Anhydrase From Neisseria GonorrhoeaeEnzymatic activity of Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae
All present enzymatic activity of Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae:
4.2.1.1; Protein crystallography data
The structure of Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae, PDB code: 8dpc
was solved by
A.K.Marapaka,
C.Das,
D.P.Flaherty,
R.Yadav,
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 Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae
(pdb code 8dpc). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae, PDB code: 8dpc: Jump to Zinc binding site number: 1; 2; 3; 4; Zinc binding site 1 out of 4 in 8dpcGo back to Zinc Binding Sites List in 8dpc
Zinc binding site 1 out
of 4 in the Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae
Mono view Stereo pair view
Zinc binding site 2 out of 4 in 8dpcGo back to Zinc Binding Sites List in 8dpc
Zinc binding site 2 out
of 4 in the Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae
Mono view Stereo pair view
Zinc binding site 3 out of 4 in 8dpcGo back to Zinc Binding Sites List in 8dpc
Zinc binding site 3 out
of 4 in the Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae
Mono view Stereo pair view
Zinc binding site 4 out of 4 in 8dpcGo back to Zinc Binding Sites List in 8dpc
Zinc binding site 4 out
of 4 in the Crystal Structure of Carbonic Anhydrase From Neisseria Gonorrhoeae
Mono view Stereo pair view
Reference:
A.K.Marapaka,
A.Nocentini,
M.S.Youse,
W.An,
K.J.Holly,
C.Das,
R.Yadav,
M.N.Seleem,
C.T.Supuran,
D.P.Flaherty.
Structural Characterization of Thiadiazolesulfonamide Inhibitors Bound to Neisseria Gonorrhoeae Alpha-Carbonic Anhydrase Acs Med.Chem.Lett. 2022.
Page generated: Sat Apr 8 08:15:53 2023
ISSN: ISSN 1948-5875 DOI: 10.1021/ACSMEDCHEMLETT.2C00471 |
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