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Atomistry » Zinc » PDB 5f8j-5fi9 » 5fdi » |
Zinc in PDB 5fdi: Crystal Structure of Human Carbonic Anhydrase II with the Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog.Enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II with the Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog.
All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase II with the Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog.:
4.2.1.1; Protein crystallography data
The structure of Crystal Structure of Human Carbonic Anhydrase II with the Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog., PDB code: 5fdi
was solved by
A.Di Fiore,
G.De Simone,
V.Alterio,
V.Riccio,
J.-Y.Winum,
F.Carta,
C.T.Supuran,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5fdi:
The structure of Crystal Structure of Human Carbonic Anhydrase II with the Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Human Carbonic Anhydrase II with the Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog.
(pdb code 5fdi). 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 II with the Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog., PDB code: 5fdi: Zinc binding site 1 out of 1 in 5fdiGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of Human Carbonic Anhydrase II with the Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog.
![]() Mono view ![]() Stereo pair view
Reference:
A.Di Fiore,
G.De Simone,
V.Alterio,
V.Riccio,
J.Y.Winum,
F.Carta,
C.T.Supuran.
The Anticonvulsant Sulfamide Jnj-26990990 and Its S,S-Dioxide Analog Strongly Inhibit Carbonic Anhydrases: Solution and X-Ray Crystallographic Studies. Org.Biomol.Chem. V. 14 4853 2016.
Page generated: Sun Oct 27 16:04:42 2024
ISSN: ESSN 1477-0539 PubMed: 27151329 DOI: 10.1039/C6OB00803H |
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