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2RUD

Solution structure of the peptidyl prolyl cis-trans isomerase domain of C113D mutant human Pin1 with sulfate ion

Summary for 2RUD
Entry DOI10.2210/pdb2rud/pdb
Related2RUC
NMR InformationBMRB: 11560
DescriptorPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (1 entity in total)
Functional Keywordsprotein/cis-trans-isomerase, ppiase, isomerase
Biological sourceHomo sapiens (human)
Cellular locationNucleus: Q13526
Total number of polymer chains1
Total formula weight13133.68
Authors
Xu, N.,Tamari, Y.,Tochio, N.,Tate, S. (deposition date: 2014-03-25, release date: 2014-12-17, Last modification date: 2023-06-14)
Primary citationXu, N.,Tochio, N.,Wang, J.,Tamari, Y.,Uewaki, J.,Utsunomiya-Tate, N.,Igarashi, K.,Shiraki, T.,Kobayashi, N.,Tate, S.
The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif.
Biochemistry, 53:5568-5578, 2014
Cited by
PubMed: 25100325
DOI: 10.1021/bi5007817
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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