› 3dyr

X-ray diffraction
2Å resolution

Crystal structure of E. coli thioredoxin mutant I76T in its oxidized form

Released:
DOI: 10.2210/pdb3dyr/pdb
PDB entry 3dyr coloured by chain, front view.
PDB entry 3dyr coloured by chain, side view.
PDB entry 3dyr coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue.
Ren G, Stephan D, Xu Z, Zheng Y, Tang D, Harrison RS, Kurz M, Jarrott R, Shouldice SR, Hiniker A, Martin JL, Heras B, Bardwell JC
J Biol Chem 284 10150-9 (2009)
PMID: 19181668

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141959 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 111 amino acids
Theoretical weight: 11.87 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AA25 (Residues: 2-109; Coverage: 99%)
Gene names: JW5856, b3781, fipA, trxA, tsnC
Sequence domains: Thioredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 58.79Å b: 39.39Å c: 90.55Å
α: 90° β: 96.63° γ: 90°
R-values:
R R work R free
0.254 0.251 0.29
Expression system: Escherichia coli

Quick links

Citations

20 review citations

How proteins form disulfide bonds.
Depuydt et al. (2011)
19 more

2 mentions without citation

Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue.
Ren et al. (2009)
1 more