2GW2
Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G
Summary for 2GW2
Entry DOI | 10.2210/pdb2gw2/pdb |
Descriptor | Peptidyl-prolyl cis-trans isomerase G, UNKNOWN ATOM OR ION (3 entities in total) |
Functional Keywords | mutation, surface mutagenesis, mutant, ppiase, cis-trans isomerization, peptidyl-prolyl isomerase, protein folding, structural genomics, structural genomics consortium, sgc, isomerase |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus matrix : Q13427 |
Total number of polymer chains | 1 |
Total formula weight | 21842.75 |
Authors | Bernstein, G.,Tempel, W.,Davis, T.,Newman, E.M.,Finerty Jr., P.J.,Mackenzie, F.,Weigelt, J.,Sundstrom, M.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Dhe-Paganon, S.,Structural Genomics Consortium (SGC) (deposition date: 2006-05-03, release date: 2006-06-13, Last modification date: 2023-08-30) |
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: 20676357DOI: 10.1371/journal.pbio.1000439 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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