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Zinc in PDB 8rj2: Crystal Structure of Carbonic Anhydrase II with N-Butyl-4-Chloro-2- (Cyclohexylsulfanyl)-5-SulfamoylbenzamideEnzymatic activity of Crystal Structure of Carbonic Anhydrase II with N-Butyl-4-Chloro-2- (Cyclohexylsulfanyl)-5-Sulfamoylbenzamide
All present enzymatic activity of Crystal Structure of Carbonic Anhydrase II with N-Butyl-4-Chloro-2- (Cyclohexylsulfanyl)-5-Sulfamoylbenzamide:
4.2.1.1; Protein crystallography data
The structure of Crystal Structure of Carbonic Anhydrase II with N-Butyl-4-Chloro-2- (Cyclohexylsulfanyl)-5-Sulfamoylbenzamide, PDB code: 8rj2
was solved by
A.Smirnov,
E.N.Manakova,
S.Grazulis,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 8rj2:
The structure of Crystal Structure of Carbonic Anhydrase II with N-Butyl-4-Chloro-2- (Cyclohexylsulfanyl)-5-Sulfamoylbenzamide also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Carbonic Anhydrase II with N-Butyl-4-Chloro-2- (Cyclohexylsulfanyl)-5-Sulfamoylbenzamide
(pdb code 8rj2). 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 Crystal Structure of Carbonic Anhydrase II with N-Butyl-4-Chloro-2- (Cyclohexylsulfanyl)-5-Sulfamoylbenzamide, PDB code: 8rj2: Zinc binding site 1 out of 1 in 8rj2Go back to Zinc Binding Sites List in 8rj2
Zinc binding site 1 out
of 1 in the Crystal Structure of Carbonic Anhydrase II with N-Butyl-4-Chloro-2- (Cyclohexylsulfanyl)-5-Sulfamoylbenzamide
Mono view Stereo pair view
Reference:
V.Paketuryte-Latve,
A.Smirnov,
E.Manakova,
L.Baranauskiene,
V.Petrauskas,
A.Zubriene,
J.Matuliene,
V.Dudutiene,
E.Capkauskaite,
A.Zaksauskas,
J.Leitans,
S.Grazulis,
K.Tars,
D.Matulis.
From X-Ray Crystallographic Structure to Intrinsic Thermodynamics of Protein-Ligand Binding Using Carbonic Anhydrase Isozymes As A Model System. Iucrj V. 11 556 2024.
Page generated: Thu Oct 31 10:31:17 2024
ISSN: ESSN 2052-2525 PubMed: 38856178 DOI: 10.1107/S2052252524004627 |
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