9GOO
Crystal structure of human carbonic anhydrase II in complex with PCI-27483
This is a non-PDB format compatible entry.
Summary for 9GOO
| Entry DOI | 10.2210/pdb9goo/pdb |
| Descriptor | Carbonic anhydrase 2, PCI-27483, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | human carbonic anhydrase ii; inhibitor; sulfonamide, metalloenzyme, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 30013.11 |
| Authors | Angeli, A.,Ferraroni, M. (deposition date: 2024-09-05, release date: 2025-09-17, Last modification date: 2026-04-01) |
| Primary citation | D'Agostino, I.,Bonardi, A.,Ferraroni, M.,Gratteri, P.,Angeli, A.,Supuran, C.T. Exploring the Polypharmacological Potential of PCI-27483: A Selective Inhibitor of Carbonic Anhydrases IX and XII. Acs Med.Chem.Lett., 15:2042-2045, 2024 Cited by PubMed Abstract: PCI-27483, originally developed as a potent and selective inhibitor of the serine protease Factor VIIa (FVIIa) in complex with tissue factor (TF), has demonstrated significant promise in cancer therapy. In addition to its primary mechanism of action, the presence of a sulfonamide moiety in the PCI-27483 structure suggests further activities through the inhibition of carbonic anhydrases (CAs), particularly the tumor-associated human (h)CA isoforms hCA IX and XII. This study investigates the inhibitory activity of PCI-27483 against the complete panel of active hCAs, highlighting its polypharmacological potential in cancer treatment. X-ray crystallography and molecular docking studies elucidated the structural features underlying its selective inhibitory activity toward hCA IX and XII, offering insights into its dual-targeting pathway. PubMed: 39563799DOI: 10.1021/acsmedchemlett.4c00443 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
Download full validation report
