› 2k18

Solution NMR

Solution structure of bb' domains of human protein disulfide isomerase

Released:
DOI: 10.2210/pdb2k18/pdb
PDB entry 2k18 coloured by chain, ensemble of 10 models, front view.
PDB entry 2k18 coloured by chain, ensemble of 10 models, side view.
PDB entry 2k18 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the bb' domains of human protein disulfide isomerase.
Denisov AY, Määttänen P, Dabrowski C, Kozlov G, Thomas DY, Gehring K
FEBS J 276 1440-9 (2009)
PMID: 19187238

Function and Biology Details

Reaction catalysed: 
Catalyzes the rearrangement of -S-S- bonds in proteins
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence 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: 228 amino acids
Theoretical weight: 25.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P07237 (Residues: 135-357; Coverage: 45%)
Gene names: ERBA2L, P4HB, PDI, PDIA1, PO4DB
Sequence domains: Thioredoxin-like domain
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

18 review citations

Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation.
Hatahet et al. (2009)
17 more

13 mentions without citation

'Something in the way she moves': The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI).
Freedman et al. (2017)
12 more