› 4nwy

X-ray diffraction
2Å resolution

Crystal structure of the b' domain of human protein disulfide isomerase-like protein of the testis (PDILT)

Released:
DOI: 10.2210/pdb4nwy/pdb
PDB entry 4nwy coloured by chain, front view.
PDB entry 4nwy coloured by chain, side view.
PDB entry 4nwy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the substrate-binding b' domain of the Protein Disulfide Isomerase-Like protein of the Testis.
Bastos-Aristizabal S, Kozlov G, Gehring K
Sci Rep 4 4464 (2014)
PMID: 24662985

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-185432 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein disulfide-isomerase-like protein of the testis Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 134 amino acids
Theoretical weight: 15.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8N807 (Residues: 258-386; Coverage: 23%)
Gene name: PDILT
Sequence domains: Thioredoxin-like domain
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand FMT 4 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21
Unit cell:
a: 60.977Å b: 119.736Å c: 33.291Å
α: 90° β: 90.9° γ: 90°
R-values:
R R work R free
0.197 0.195 0.238
Expression system: Escherichia coli BL21

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Citations

3 mentions without citation

Functions and mechanisms of protein disulfide isomerase family in cancer emergence.
Rahman et al. (2022)
2 more