2HAQ
Crystal Structure of Cyclophilin A from Leishmania Donovani
Summary for 2HAQ
| Entry DOI | 10.2210/pdb2haq/pdb |
| Descriptor | Cyclophilin (2 entities in total) |
| Functional Keywords | cyclophilin, rotamase, proline, isomerase, cis-trans, protozoa, leishmania, donovani, kala-azar. |
| Biological source | Leishmania donovani |
| Total number of polymer chains | 1 |
| Total formula weight | 19090.54 |
| Authors | Venugopal, V.,Sen, B.,Datta, A.K.,Banerjee, R. (deposition date: 2006-06-13, release date: 2006-06-20, Last modification date: 2023-08-30) |
| Primary citation | Venugopal, V.,Sen, B.,Datta, A.K.,Banerjee, R. Structure of cyclophilin from Leishmania donovani at 1.97 A resolution. Acta Crystallogr.,Sect.F, 63:60-64, 2007 Cited by PubMed Abstract: The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 A resolution to a crystallographic R factor of 0.178 (R(free) = 0.197). The structure was solved by molecular replacement using cyclophilin from Trypanosoma cruzi as the search model. LdCyp exhibits complete structural conservation of the cyclosporin-binding site with respect to the homologous human protein, as anticipated from LdCyp-cyclosporin binding studies. Comparisons with other cyclophilins show deviations primarily in the loop regions. The solvent structure encompassing the molecule has also been analyzed in some detail. PubMed: 17277440DOI: 10.1107/S1744309106056351 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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