4XNC
Crystal structure at room temperature of cyclophilin D in complex with an inhibitor
Summary for 4XNC
| Entry DOI | 10.2210/pdb4xnc/pdb |
| Descriptor | Peptidyl-prolyl cis-trans isomerase F, mitochondrial, ethyl N-[(4-aminobenzyl)carbamoyl]glycinate (3 entities in total) |
| Functional Keywords | inhibitor isomerase fragment based drug design, isomerase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Mitochondrion matrix : P30405 |
| Total number of polymer chains | 1 |
| Total formula weight | 17903.41 |
| Authors | Gelin, M.,Allemand, F.,Labesse, G.,Guichou, J.F. (deposition date: 2015-01-15, release date: 2015-08-12, Last modification date: 2024-05-08) |
| Primary citation | Gelin, M.,Delfosse, V.,Allemand, F.,Hoh, F.,Sallaz-Damaz, Y.,Pirocchi, M.,Bourguet, W.,Ferrer, J.L.,Labesse, G.,Guichou, J.F. Combining `dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography. Acta Crystallogr.,Sect.D, 71:1777-1787, 2015 Cited by PubMed Abstract: X-ray crystallography is an established technique for ligand screening in fragment-based drug-design projects, but the required manual handling steps - soaking crystals with ligand and the subsequent harvesting - are tedious and limit the throughput of the process. Here, an alternative approach is reported: crystallization plates are pre-coated with potential binders prior to protein crystallization and X-ray diffraction is performed directly 'in situ' (or in-plate). Its performance is demonstrated on distinct and relevant therapeutic targets currently being studied for ligand screening by X-ray crystallography using either a bending-magnet beamline or a rotating-anode generator. The possibility of using DMSO stock solutions of the ligands to be coated opens up a route to screening most chemical libraries. PubMed: 26249358DOI: 10.1107/S1399004715010342 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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