6RW1
Crystal structure of hCA II in complex with Urea, N-(1,3-dihydro-1-hydroxy-2,1-benzoxaborol-6-yl)-N'-(phenylmethyl)-
Summary for 6RW1
| Entry DOI | 10.2210/pdb6rw1/pdb |
| Related | 1CA2 |
| Descriptor | Carbonic anhydrase 2, ZINC ION, 1-[7,7-bis(oxidanyl)-8-oxa-7-boranuidabicyclo[4.3.0]nona-1(6),2,4-trien-4-yl]-3-(phenylmethyl)thiourea, ... (4 entities in total) |
| Functional Keywords | protein-inhibitor binding, lyase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 29857.89 |
| Authors | Di Fiore, A.,De Simone, G. (deposition date: 2019-06-03, release date: 2019-08-28, Last modification date: 2024-01-24) |
| Primary citation | Langella, E.,Alterio, V.,D'Ambrosio, K.,Cadoni, R.,Winum, J.Y.,Supuran, C.T.,Monti, S.M.,De Simone, G.,Di Fiore, A. Exploring benzoxaborole derivatives as carbonic anhydrase inhibitors: a structural and computational analysis reveals their conformational variability as a tool to increase enzyme selectivity. J Enzyme Inhib Med Chem, 34:1498-1505, 2019 Cited by PubMed Abstract: Recent studies identified the benzoxaborole moiety as a new zinc-binding group able to interact with carbonic anhydrase (CA) active site. Here, we report a structural analysis of benzoxaboroles containing urea/thiourea groups, showing that these molecules are very versatile since they can bind the enzyme assuming different binding conformations and coordination geometries of the catalytic zinc ion. In addition, theoretical calculations of binding free energy were performed highlighting the key role of specific residues for protein-inhibitor recognition. Overall, these data are very useful for the development of new inhibitors with higher selectivity and efficacy for various CAs. PubMed: 31423863DOI: 10.1080/14756366.2019.1653291 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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