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Solution NMR

Solution structure of the apo form of human glutaredoxin 5

Released:
DOI: 10.2210/pdb2mmz/pdb
PDB entry 2mmz coloured by chain, ensemble of 20 models, front view.
PDB entry 2mmz coloured by chain, ensemble of 20 models, side view.
PDB entry 2mmz coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
[2Fe-2S] cluster transfer in iron-sulfur protein biogenesis.
Banci L, Brancaccio D, Ciofi-Baffoni S, Del Conte R, Gadepalli R, Mikolajczyk M, Neri S, Piccioli M, Winkelmann J
Proc Natl Acad Sci U S A 111 6203-8 (2014)
PMID: 24733926

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaredoxin-related protein 5, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q86SX6 (Residues: 35-150; Coverage: 74%)
Gene names: C14orf87, GLRX5
Sequence domains: Glutaredoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: molecular dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

Mammalian iron-sulphur proteins: novel insights into biogenesis and function.
Rouault TA. (2015)
16 more

6 mentions without citation

Glutaredoxin: Discovery, redox defense and much more.
Ogata et al. (2021)
5 more