› 2yjz

X-ray diffraction
2.2Å resolution

Rat STEAP4 oxidoreductase domain complexed with NADP

Released:
DOI: 10.2210/pdb2yjz/pdb
PDB entry 2yjz coloured by chain, front view.
PDB entry 2yjz coloured by chain, side view.
PDB entry 2yjz coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The crystal structure of six-transmembrane epithelial antigen of the prostate 4 (Steap4), a ferri/cuprireductase, suggests a novel interdomain flavin-binding site.
Gauss GH, Kleven MD, Sendamarai AK, Fleming MD, Lawrence CM
J Biol Chem 288 20668-82 (2013)
PMID: 23733181

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175763 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metalloreductase STEAP4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 201 amino acids
Theoretical weight: 22.01 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4V8K1 (Residues: 1-195; Coverage: 42%)
Gene name: Steap4
Sequence domains: NADP oxidoreductase coenzyme F420-dependent
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

2 bound ligands:
Ligand NAP 4 x NAP
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 69.228Å b: 85.111Å c: 128.035Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.203 0.238
Expression system: Escherichia coli

Quick links

Citations

9 review citations

STEAP4: its emerging role in metabolism and homeostasis of cellular iron and copper.
Scarl et al. (2017)
8 more

2 mentions without citation

The crystal structure of six-transmembrane epithelial antigen of the prostate 4 (Steap4), a ferri/cuprireductase, suggests a novel interdomain flavin-binding site.
Gauss et al. (2013)
1 more