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Atomistry » Zinc » PDB 4q47-4q8w » 4q6e » |
Zinc in PDB 4q6e: Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{[3- (3,5-Dimethyl-1H-Pyrazol-1-Yl)-3-Oxopropyl]Amino}Benzene-1- SulfonamideEnzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{[3- (3,5-Dimethyl-1H-Pyrazol-1-Yl)-3-Oxopropyl]Amino}Benzene-1- Sulfonamide
All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{[3- (3,5-Dimethyl-1H-Pyrazol-1-Yl)-3-Oxopropyl]Amino}Benzene-1- Sulfonamide:
4.2.1.1; Protein crystallography data
The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{[3- (3,5-Dimethyl-1H-Pyrazol-1-Yl)-3-Oxopropyl]Amino}Benzene-1- Sulfonamide, PDB code: 4q6e
was solved by
A.Smirnov,
E.Manakova,
S.Grazulis,
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 Human Carbonic Anhydrase Isozyme II with 4-{[3- (3,5-Dimethyl-1H-Pyrazol-1-Yl)-3-Oxopropyl]Amino}Benzene-1- Sulfonamide
(pdb code 4q6e). 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 Human Carbonic Anhydrase Isozyme II with 4-{[3- (3,5-Dimethyl-1H-Pyrazol-1-Yl)-3-Oxopropyl]Amino}Benzene-1- Sulfonamide, PDB code: 4q6e: Zinc binding site 1 out of 1 in 4q6eGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{[3- (3,5-Dimethyl-1H-Pyrazol-1-Yl)-3-Oxopropyl]Amino}Benzene-1- Sulfonamide
![]() Mono view ![]() Stereo pair view
Reference:
K.Rutkauskas,
A.Zubriene,
I.Tumosiene,
K.Kantminiene,
M.Kazemekaite,
A.Smirnov,
J.Kazokaite,
V.Morkunaite,
E.Capkauskaite,
E.Manakova,
S.Grazulis,
Z.J.Beresnevicius,
D.Matulis.
4-Amino-Substituted Benzenesulfonamides As Inhibitors of Human Carbonic Anhydrases. Molecules V. 19 17356 2014.
Page generated: Sun Oct 27 06:17:13 2024
ISSN: ESSN 1420-3049 PubMed: 25353386 DOI: 10.3390/MOLECULES191117356 |
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