› 1h75

X-ray diffraction
1.7Å resolution

Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like protein NrdH-redoxin from Escherichia coli.

Released:
DOI: 10.2210/pdb1h75/pdb
PDB entry 1h75 coloured by chain, front view.
PDB entry 1h75 coloured by chain, side view.
PDB entry 1h75 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like NrdH-redoxin from Escherichia coli.
Stehr M, Schneider G, Aslund F, Holmgren A, Lindqvist Y
J Biol Chem 276 35836-41 (2001)
PMID: 11441020

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaredoxin-like protein NrdH Chain: A
Molecule details ›
Chain: A
Length: 81 amino acids
Theoretical weight: 9.15 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AC65 (Residues: 1-81; Coverage: 100%)
Gene names: JW2648, b2673, nrdH, ygaN
Sequence domains: Glutaredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P212121
Unit cell:
a: 31.151Å b: 41.346Å c: 58.668Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.211
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.
Fernandes et al. (2004)
1 more

7 mentions without citation

Structure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site.
Couturier et al. (2009)
6 more