› 3qwa

X-ray diffraction
2Å resolution

Crystal structure of Saccharomyces cerevisiae Zeta-crystallin-like quinone oxidoreductase Zta1

Released:
DOI: 10.2210/pdb3qwa/pdb
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Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural insights into the cofactor-assisted substrate recognition of yeast quinone oxidoreductase Zta1.
Guo PC, Ma XX, Bao ZZ, Ma JD, Chen Y, Zhou CZ
J Struct Biol 176 112-8 (2011)
PMID: 21820057

Function and Biology Details

Reaction catalysed: 
NADPH + 2 quinone = NADP(+) + 2 semiquinone
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable quinone oxidoreductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 334 amino acids
Theoretical weight: 37.06 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P38230 (Residues: 1-334; Coverage: 100%)
Gene names: YBR0421, YBR046C, ZTA1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 74.97Å b: 87.313Å c: 100.514Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.247
Expression system: Escherichia coli

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Citations

9 citation in other articles

YNL134C from Saccharomyces cerevisiae encodes a novel protein with aldehyde reductase activity for detoxification of furfural derived from lignocellulosic biomass.
Zhao et al. (2015)
8 more

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