› 1erv

X-ray diffraction
1.65Å resolution

HUMAN THIOREDOXIN MUTANT WITH CYS 73 REPLACED BY SER (REDUCED FORM)

Released:
DOI: 10.2210/pdb1erv/pdb
PDB entry 1erv coloured by chain, front view.
PDB entry 1erv coloured by chain, side view.
PDB entry 1erv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.
Weichsel A, Gasdaska JR, Powis G, Montfort WR
Structure 4 735-51 (1996)
PMID: 8805557

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145351 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10599 (Residues: 1-105; Coverage: 100%)
Gene names: TRDX, TRX, TRX1, TXN
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 67.8Å b: 26.33Å c: 51.54Å
α: 90° β: 95.04° γ: 90°
R-values:
R R work R free
0.21 0.21 0.24
Expression system: Escherichia coli

Quick links

Citations

41 review citations

Physiological functions of thioredoxin and thioredoxin reductase.
Arnér et al. (2000)
40 more

10 mentions without citation

An accurate, residue-level, pair potential of mean force for folding and binding based on the distance-scaled, ideal-gas reference state.
Zhang et al. (2004)
9 more