1fjd Summary

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HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14

The structure was published by Terada, T., Shirouzu, M., Fukumori, Y., et al., Kigawa, T., Yokoyama, S., and Uchida, T., in 2001 in a paper entitled "Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2000.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of PEPTIDYL PROLYL CIS/TRANS ISOMERASE (PPIASE). This molecule has the UniProt identifier Q9Y237 (PIN4_HUMAN)search. The sample contained 104 residues which is < 90% of the natural sequence. Out of 104 residues 104 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PEPTIDYL PROLYL CIS/TRANS ISOMERASE (PPIASE) Q9Y237 (28-131) (PIN4_HUMAN)search Homo sapienssearch < 90% 104 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9Y237 (28 - 131) PEPTIDYL PROLYL CIS/TRANS ISOMERASE (PPIASE) Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A FKBP immunophilin/proline isomerasesearch Chitinase A; domain 3search PPIC-type PPIASE domainsearch

Chain ID Molecular function (GO)
A (Q9Y237) isomerase activitysearch

Chain InterPro annotation
A Peptidyl-prolyl cis-trans isomerase, PpiC-typesearch