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Atomistry » Zinc » PDB 1g45-1gkq » 1g4j » |
Zinc in PDB 1g4j: Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 3,4,5,6-Pentafluorophenyl)Methyl]-BenzamideEnzymatic activity of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 3,4,5,6-Pentafluorophenyl)Methyl]-Benzamide
All present enzymatic activity of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 3,4,5,6-Pentafluorophenyl)Methyl]-Benzamide:
4.2.1.1; Protein crystallography data
The structure of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 3,4,5,6-Pentafluorophenyl)Methyl]-Benzamide, PDB code: 1g4j
was solved by
C.-Y.Kim,
J.S.Chang,
J.B.Doyon,
T.T.Baird Jr.,
C.A.Fierke,
A.Jain,
D.W.Christianson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1g4j:
The structure of Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 3,4,5,6-Pentafluorophenyl)Methyl]-Benzamide also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 3,4,5,6-Pentafluorophenyl)Methyl]-Benzamide
(pdb code 1g4j). 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 (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 3,4,5,6-Pentafluorophenyl)Methyl]-Benzamide, PDB code: 1g4j: Zinc binding site 1 out of 1 in 1g4jGo back to Zinc Binding Sites List in 1g4j
Zinc binding site 1 out
of 1 in the Carbonic Anhydrase II (F131V) Complexed with 4-(Aminosulfonyl)-N-[(2, 3,4,5,6-Pentafluorophenyl)Methyl]-Benzamide
Mono view Stereo pair view
Reference:
C.-Y.Kim,
J.S.Chang,
J.B.Doyon,
T.T.Baird Jr.,
C.A.Fierke,
A.Jain,
D.W.Christianson.
Contribution of Flourine to Protein-Ligand Affinity in the Binding of Flouroaromatic Inhibitors to Carbonic Anhydrase II J.Am.Chem.Soc. V. 122 12125 2000.
Page generated: Wed Dec 16 02:49:53 2020
ISSN: ISSN 0002-7863 DOI: 10.1021/JA002627N |
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