1EQ3
NMR STRUCTURE OF HUMAN PARVULIN HPAR14
Summary for 1EQ3
Entry DOI | 10.2210/pdb1eq3/pdb |
Related | 1PIN |
Descriptor | PEPTIDYL-PROLYL CIS/TRANS ISOMERASE (PPIASE) (1 entity in total) |
Functional Keywords | peptidyl-prolyl cis-trans isomerase, parvulin, isomerase |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 10731.55 |
Authors | Sekerina, E.,Rahfeld, U.J.,Muller, J.,Fischer, G.,Bayer, P. (deposition date: 2000-04-02, release date: 2001-04-04, Last modification date: 2024-05-22) |
Primary citation | Sekerina, E.,Rahfeld, J.U.,Muller, J.,Fanghanel, J.,Rascher, C.,Fischer, G.,Bayer, P. NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein. J.Mol.Biol., 301:1003-1017, 2000 Cited by PubMed: 10966801DOI: 10.1006/jmbi.2000.4013 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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