1ZKC

Crystal Structure of the cyclophiln_RING domain of human peptidylprolyl isomerase (cyclophilin)-like 2 isoform b

Summary for 1ZKC

Entry DOI	10.2210/pdb1zkc/pdb
Descriptor	Peptidyl-prolyl cis-trans isomerase like 2, BETA-MERCAPTOETHANOL (3 entities in total)
Functional Keywords	cis-trans isomerization, peptidylprolyl isomerase, protein-folding, structural genomics consortium, sgc, isomerase
Biological source	Homo sapiens (human)
Cellular location	Nucleus : Q13356
Total number of polymer chains	2
Total formula weight	44493.99
Authors	Walker, J.R.,Davis, T.,Newman, E.M.,Mackenzie, F.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.,Edwards, A.,Bochkarev, A.,Dhe-Paganon, S.,Structural Genomics Consortium (SGC) (deposition date: 2005-05-02, release date: 2005-08-16, Last modification date: 2023-08-23)
Primary citation	Davis, T.L.,Walker, J.R.,Campagna-Slater, V.,Finerty, P.J.,Paramanathan, R.,Bernstein, G.,MacKenzie, F.,Tempel, W.,Ouyang, H.,Lee, W.H.,Eisenmesser, E.Z.,Dhe-Paganon, S. Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PLoS Biol., 8:e1000439-e1000439, 2010 Cited by PubMed: 20676357 DOI: 10.1371/journal.pbio.1000439 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.65 Å)

Structure validation