3N4B

Crystal structure of human carbonic anhydrase II in complex with a benzenesulfonamide inhibitor

Summary for 3N4B

Entry DOI	10.2210/pdb3n4b/pdb
Related	3MZC 3N0N 3N2P 3N3J
Descriptor	Carbonic anhydrase 2, ZINC ION, 4-{[(4-fluorophenyl)carbamoyl]amino}benzenesulfonamide, ... (5 entities in total)
Functional Keywords	lyase, zinc metalloenzyme, zinc ligands, benzenesulfonamide, inhibitor, lyase-lyase inhibitor complex, lyase/lyase inhibitor
Biological source	Homo sapiens
Cellular location	Cytoplasm : P00918
Total number of polymer chains	1
Total formula weight	29755.88
Authors	Avvaru, B.S.,Wagner, J.,Robbins, A.H.,McKenna, R. (deposition date: 2010-05-21, release date: 2011-03-09, Last modification date: 2023-09-06)
Primary citation	Pacchiano, F.,Aggarwal, M.,Avvaru, B.S.,Robbins, A.H.,Scozzafava, A.,McKenna, R.,Supuran, C.T. Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency. Chem.Commun.(Camb.), 46:8371-8373, 2010 Cited by PubMed Abstract: 4-Substituted-ureido benzenesulfonamides showing inhibitory activity against carbonic anhydrase (CA, EC 4.2.1.1) II between 3.3-226 nM were crystallized in complex with the enzyme. Hydrophobic interactions between the scaffold of the inhibitors in different hydrophobic pockets of the enzyme were observed, explaining the diverse inhibitory range of these derivatives. PubMed: 20922253 DOI: 10.1039/c0cc02707c PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation