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Atomistry » Zinc » PDB 3m1k-3m6o » 3m3x » |
Zinc in PDB 3m3x: Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{2-[N- (6-Methoxy-5-Nitropyrimidin-4-Yl)Amino]Ethyl}BenzenesulfonamideEnzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{2-[N- (6-Methoxy-5-Nitropyrimidin-4-Yl)Amino]Ethyl}Benzenesulfonamide
All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{2-[N- (6-Methoxy-5-Nitropyrimidin-4-Yl)Amino]Ethyl}Benzenesulfonamide:
4.2.1.1; Protein crystallography data
The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{2-[N- (6-Methoxy-5-Nitropyrimidin-4-Yl)Amino]Ethyl}Benzenesulfonamide, PDB code: 3m3x
was solved by
S.Grazulis,
E.Manakova,
D.Golovenko,
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-{2-[N- (6-Methoxy-5-Nitropyrimidin-4-Yl)Amino]Ethyl}Benzenesulfonamide
(pdb code 3m3x). 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-{2-[N- (6-Methoxy-5-Nitropyrimidin-4-Yl)Amino]Ethyl}Benzenesulfonamide, PDB code: 3m3x: Zinc binding site 1 out of 1 in 3m3xGo back to Zinc Binding Sites List in 3m3x
Zinc binding site 1 out
of 1 in the Crystal Structure of Human Carbonic Anhydrase Isozyme II with 4-{2-[N- (6-Methoxy-5-Nitropyrimidin-4-Yl)Amino]Ethyl}Benzenesulfonamide
Mono view Stereo pair view
Reference:
J.Sudzius,
L.Baranauskiene,
D.Golovenko,
J.Matuliene,
V.Michailoviene,
J.Torresan,
J.Jachno,
R.Sukackaite,
E.Manakova,
S.Grazulis,
S.Tumkevicius,
D.Matulis.
4-[N-(Substituted 4-Pyrimidinyl)Amino]Benzenesulfonamides As Inhibitors of Carbonic Anhydrase Isozymes I, II, VII, and XIII Bioorg.Med.Chem. V. 18 7413 2010.
Page generated: Wed Dec 16 04:34:04 2020
ISSN: ISSN 0968-0896 PubMed: 20889345 DOI: 10.1016/J.BMC.2010.09.011 |
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