› 3bj5

X-ray diffraction
2.2Å resolution

Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain

Released:
DOI: 10.2210/pdb3bj5/pdb
PDB entry 3bj5 coloured by chain, front view.
PDB entry 3bj5 coloured by chain, side view.
PDB entry 3bj5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain.
Nguyen VD, Wallis K, Howard MJ, Haapalainen AM, Salo KE, Saaranen MJ, Sidhu A, Wierenga RK, Freedman RB, Ruddock LW, Williamson RA
J Mol Biol 383 1144-55 (2008)
PMID: 18801374

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: 147 amino acids
Theoretical weight: 17.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07237 (Residues: 230-368; Coverage: 28%)
Gene names: ERBA2L, P4HB, PDI, PDIA1, PO4DB
Sequence domains: Thioredoxin-like domain
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P3121
Unit cell:
a: 57.37Å b: 57.37Å c: 68.31Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.194 0.255
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

9 mentions without citation

S-nitrosylation of the thioredoxin-like domains of protein disulfide isomerase and its role in neurodegenerative conditions.
Conway et al. (2015)
8 more