› 1jhb

Solution NMR

HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES

Released:
DOI: 10.2210/pdb1jhb/pdb
PDB entry 1jhb coloured by chain, ensemble of 20 models, front view.
PDB entry 1jhb coloured by chain, ensemble of 20 models, side view.
PDB entry 1jhb coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The NMR solution structure of human glutaredoxin in the fully reduced form.
Sun C, Berardi MJ, Bushweller JH
J Mol Biol 280 687-701 (1998)
PMID: 9677297

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-153015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaredoxin-1 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35754 (Residues: 1-106; Coverage: 100%)
Gene names: GLRX, GRX
Sequence domains: Glutaredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

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Citations

7 review citations

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

16 mentions without citation

Thiol redox biochemistry: insights from computer simulations.
Zeida et al. (2014)
15 more