› 1mek

Solution NMR

HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES

Released:
DOI: 10.2210/pdb1mek/pdb
PDB entry 1mek coloured by chain, ensemble of 40 models, front view.
PDB entry 1mek coloured by chain, ensemble of 40 models, side view.
PDB entry 1mek coloured by chain, ensemble of 40 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE
Biochemistry 35 7684-91 (1996)
PMID: 8672469

Function and Biology Details

Reaction catalysed: 
Catalyzes the rearrangement of -S-S- bonds in proteins
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein disulfide-isomerase Chain: A
Molecule details ›
Chain: A
Length: 120 amino acids
Theoretical weight: 13.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07237 (Residues: 18-137; Coverage: 24%)
Gene names: ERBA2L, P4HB, PDI, PDIA1, PO4DB
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

28 review citations

The human protein disulphide isomerase family: substrate interactions and functional properties.
Ellgaard et al. (2005)
27 more

18 mentions without citation

Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase.
Cheng et al. (2011)
17 more