2EU2
Human Carbonic Anhydrase II in complex with novel inhibitors
Summary for 2EU2
| Entry DOI | 10.2210/pdb2eu2/pdb |
| Related | 2EU3 |
| Descriptor | Carbonic anhydrase 2, ZINC ION, (R)-1-AMINO-1-[5-(DIMETHYLAMINO)-1,3,4-THIADIAZOL-2-YL]METHANESULFONAMIDE, ... (4 entities in total) |
| Functional Keywords | carbonic anhydrase ii proton transfer inhibitor, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 29591.77 |
| Authors | Fisher, S.Z.,Govindasamy, L.,Boyle, N.,Agbandje-McKenna, M.,Silverman, D.N.,Blackburn, G.M.,McKenna, R. (deposition date: 2005-10-28, release date: 2006-07-11, Last modification date: 2023-08-23) |
| Primary citation | Fisher, S.Z.,Govindasamy, L.,Boyle, N.,Agbandje-McKenna, M.,Silverman, D.N.,Blackburn, G.M.,McKenna, R. X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes. Acta Crystallogr.,Sect.F, 62:618-622, 2006 Cited by PubMed Abstract: Human carbonic anhydrases (CAs) are well studied targets for the development of inhibitors for pharmaceutical applications. The crystal structure of human CA II has been determined in complex with two CA inhibitors (CAIs) containing conventional sulfonamide and thiadiazole moieties separated by a -CF2- or -CHNH2- spacer group. The structures presented here reveal that these spacer groups allow novel binding modes for the thiadiazole moiety compared with conventional CAIs. PubMed: 16820676DOI: 10.1107/S1744309106020446 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
Download full validation report
