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Atomistry » Zinc » PDB 4yn2-4z1d » 4yxi | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4yn2-4z1d » 4yxi » |
Zinc in PDB 4yxi: Human Carbonic Anhydrase II Complexed with An Inhibitor with A Benzenesulfonamide Group (2).Enzymatic activity of Human Carbonic Anhydrase II Complexed with An Inhibitor with A Benzenesulfonamide Group (2).
All present enzymatic activity of Human Carbonic Anhydrase II Complexed with An Inhibitor with A Benzenesulfonamide Group (2).:
4.2.1.1; Protein crystallography data
The structure of Human Carbonic Anhydrase II Complexed with An Inhibitor with A Benzenesulfonamide Group (2)., PDB code: 4yxi
was solved by
C.Rechlin,
A.Heine,
G.Klebe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4yxi:
The structure of Human Carbonic Anhydrase II Complexed with An Inhibitor with A Benzenesulfonamide Group (2). also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Human Carbonic Anhydrase II Complexed with An Inhibitor with A Benzenesulfonamide Group (2).
(pdb code 4yxi). 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 Human Carbonic Anhydrase II Complexed with An Inhibitor with A Benzenesulfonamide Group (2)., PDB code: 4yxi: Zinc binding site 1 out of 1 in 4yxiGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Human Carbonic Anhydrase II Complexed with An Inhibitor with A Benzenesulfonamide Group (2).
![]() Mono view ![]() Stereo pair view
Reference:
R.Gaspari,
C.Rechlin,
A.Heine,
G.Bottegoni,
W.Rocchia,
D.Schwarz,
J.Bomke,
H.D.Gerber,
G.Klebe,
A.Cavalli.
Kinetic and Structural Insights Into the Mechanism of Binding of Sulfonamides to Human Carbonic Anhydrase By Computational and Experimental Studies. J.Med.Chem. V. 59 4245 2016.
Page generated: Sun Oct 27 11:30:39 2024
ISSN: ISSN 0022-2623 PubMed: 26700575 DOI: 10.1021/ACS.JMEDCHEM.5B01643 |
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