› 1ego

Solution NMR

NMR STRUCTURE OF OXIDIZED ESCHERICHIA COLI GLUTAREDOXIN: COMPARISON WITH REDUCED E. COLI GLUTAREDOXIN AND FUNCTIONALLY RELATED PROTEINS

Released:
DOI: 10.2210/pdb1ego/pdb
PDB entry 1ego coloured by chain, ensemble of 20 models, front view.
PDB entry 1ego coloured by chain, ensemble of 20 models, side view.
PDB entry 1ego coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Xia TH, Bushweller JH, Sodano P, Billeter M, Björnberg O, Holmgren A, Wüthrich K
Protein Sci 1 310-21 (1992)
PMID: 1304339

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159495 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaredoxin 1 Chain: A
Molecule details ›
Chain: A
Length: 85 amino acids
Theoretical weight: 9.7 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P68688 (Residues: 1-85; Coverage: 100%)
Gene names: JW0833, b0849, grx, grxA
Sequence domains: Glutaredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

17 review citations

Thioredoxin--a fold for all reasons.
Martin JL. (1995)
16 more

8 mentions without citation

The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution.
Hatori et al. (2016)
7 more