4E49

Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors

Summary for 4E49

Entry DOI	10.2210/pdb4e49/pdb
Related	4E3D 4E3F 4E3G 4E3H 4E4A
Descriptor	Carbonic anhydrase 2, ZINC ION, MERCURIBENZOIC ACID, ... (6 entities in total)
Functional Keywords	carbonate dehydratase, inhibitor, lyase-lyase inhibitor complex, lyase/lyase inhibitor
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm: P00918
Total number of polymer chains	1
Total formula weight	30212.68
Authors	Cohen, S.M.,Martin, D.P. (deposition date: 2012-03-12, release date: 2012-06-27, Last modification date: 2023-11-08)
Primary citation	Martin, D.P.,Cohen, S.M. Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors Chem.Commun.(Camb.), 48:5259-5261, 2012 Cited by PubMed Abstract: A series of hydroxybenzoic acid derivatives have shown inhibitory activity against carbonic anhydrase (CA). X-ray crystallography shows that these molecules inhibit not by binding the active site metal ion but by strong hydrogen bonding to the metal-bound water nucleophile. The binding mode observed for these molecules is distinct when compared to other non-metal-binding CA inhibitors. PubMed: 22531842 DOI: 10.1039/c2cc32013d PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.45 Å)

Structure validation