2WFI

Atomic resolution crystal structure of the PPIase domain of human cyclophilin G

Summary for 2WFI

Entry DOI	10.2210/pdb2wfi/pdb
Related	2GW2 2WFJ
Descriptor	PEPTIDYL-PROLYL CIS-TRANS ISOMERASE G, MAGNESIUM ION (3 entities in total)
Functional Keywords	phosphoprotein, pre-mrna splicing, alternative splicing, nucleus, rotamase, isomerase, cyclosporin, peptidyl-prolyl cis-trans isomerase
Biological source	HOMO SAPIENS (HUMAN)
Total number of polymer chains	1
Total formula weight	19940.13
Authors	Stegmann, C.M.,Sheldrick, G.M.,Wahl, M.C. (deposition date: 2009-04-06, release date: 2009-06-16, Last modification date: 2025-04-09)
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