2WFJ

Atomic resolution crystal structure of the PPIase domain of human cyclophilin G in complex with cyclosporin A.

Summary for 2WFJ

Entry DOI	10.2210/pdb2wfj/pdb
Related	1BCK 1C5F 1CSA 1CWA 1CWB 1CWC 1CWF 1CWH 1CWI 1CWJ 1CWK 1CWL 1CWM 1CWO 1CYA 1CYB 1CYN 1IKF 1M63 1MF8 1MIK 1QNG 1QNH 1XQ7 2ESL 2GW2 2OJU 2POY 2RMA 2RMB 2RMC 2WFI 2X2C 2X7K 2Z6W 3BO7 3CYS 3EOV
Related PRD ID	PRD_000142
Descriptor	PEPTIDYL-PROLYL CIS-TRANS ISOMERASE G, CYCLOSPORIN A, 1,2-ETHANEDIOL, ... (6 entities in total)
Functional Keywords	isomerase-immunosuppressant complex, cyclophilin-cyclosporin complex, cyclosporin a, immunosuppressant, cyclophilin, isomerase/immunosuppressant
Biological source	HOMO SAPIENS (HUMAN) More
Total number of polymer chains	2
Total formula weight	21210.27
Authors	Stegmann, C.M.,Sheldrick, G.M.,Wahl, M.C. (deposition date: 2009-04-06, release date: 2009-06-16, Last modification date: 2019-05-22)
Primary citation	Stegmann, C.M.,Seeliger, D.,Sheldrick, G.M.,De Groot, B.L.,Wahl, M.C. The Thermodynamic Influence of Trapped Water Molecules on a Protein-Ligand Interaction. Angew.Chem.Int.Ed.Engl., 48:5207-, 2009 Cited by PubMed Abstract: Water molecules doing time: Atomic-resolution crystal structures of the PPIase domain of cyclophilin G, alone and in complex with cyclosporin A, and together with MD simulations and calorimetry, reveal how trapped water molecules influence the thermodynamic profile of a protein-ligand interaction. PubMed: 19499554 DOI: 10.1002/ANIE.200900481 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (0.75 Å)

Structure validation