› 4ooa

X-ray diffraction
1.58Å resolution

CRYSTAL STRUCTURE of NAF1 (MINER1): H114C THE REDOX-ACTIVE 2FE-2S PROTEIN

Released:
DOI: 10.2210/pdb4ooa/pdb
PDB entry 4ooa coloured by chain, front view.
PDB entry 4ooa coloured by chain, side view.
PDB entry 4ooa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A point mutation in the [2Fe-2S] cluster binding region of the NAF-1 protein (H114C) dramatically hinders the cluster donor properties.
Tamir S, Eisenberg-Domovich Y, Conlan AR, Stofleth JT, Lipper CH, Paddock ML, Mittler R, Jennings PA, Livnah O, Nechushtai R
Acta Crystallogr D Biol Crystallogr 70 1572-8 (2014)
PMID: 24914968

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185405 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CDGSH iron-sulfur domain-containing protein 2 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 68 amino acids
Theoretical weight: 7.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8N5K1 (Residues: 68-135; Coverage: 50%)
Gene names: CDGSH2, CISD2, ERIS, ZCD2
Sequence domains: Iron-binding zinc finger CDGSH type
Structure domains: CDGSH iron-sulfur domain, mitoNEET-type

Ligands and Environments

1 bound ligand:
Ligand FES 6 x FES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 48.393Å b: 60.985Å c: 135.241Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.196
Expression system: Escherichia coli

Quick links

Citations

2 review citations

NEET Proteins: A New Link Between Iron Metabolism, Reactive Oxygen Species, and Cancer.
Mittler et al. (2019)
1 more

1 mention without citation

A point mutation in the [2Fe-2S] cluster binding region of the NAF-1 protein (H114C) dramatically hinders the cluster donor properties.
Tamir et al. (2014)