1mek Summary

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HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES

The structure was published by Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M., and Creighton, T.E., in 1996 in a paper entitled "Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1996.

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

The PDB entry contains the structure of PROTEIN DISULFIDE ISOMERASE. This molecule has the UniProt identifier P07237 (PDIA1_HUMAN)search. The sample contained 120 residues which is < 90% of the natural sequence. Out of 120 residues 120 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 PROTEIN DISULFIDE ISOMERASE P07237 (18-137) (PDIA1_HUMAN)search Homo sapienssearch 94% 120 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07237 (18 - 137) PROTEIN DISULFIDE ISOMERASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P07237) PDI-likesearch Glutaredoxinsearch PF00085: Thioredoxinsearch

Chain ID Biological process (GO) Molecular function (GO)
A (P07237) cell redox homeostasissearch glycerol ether metabolic processsearch isomerase activitysearch electron carrier activitysearch protein disulfide oxidoreductase activitysearch

Chain InterPro annotation
A Thioredoxinsearch Disulphide isomerasesearch Thioredoxin-like foldsearch Thioredoxin domainsearch Thioredoxin, conserved sitesearch