1PIN
PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
Summary for 1PIN
Entry DOI | 10.2210/pdb1pin/pdb |
Descriptor | PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, ALANINE, PROLINE, ... (6 entities in total) |
Functional Keywords | peptidyl-prolyl cis-trans isomerase, rotamase, complex (isomerase-dipeptide), isomerase |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: Q13526 |
Total number of polymer chains | 1 |
Total formula weight | 19076.21 |
Authors | Noel, J.P.,Ranganathan, R.,Hunter, T. (deposition date: 1998-06-21, release date: 1998-10-14, Last modification date: 2024-05-22) |
Primary citation | Ranganathan, R.,Lu, K.P.,Hunter, T.,Noel, J.P. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell(Cambridge,Mass.), 89:875-886, 1997 Cited by PubMed: 9200606DOI: 10.1016/S0092-8674(00)80273-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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