› 5mp4

X-ray diffraction
2.79Å resolution

The structure of Pst2p from Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb5mp4/pdb
PDB entry 5mp4 coloured by chain, front view.
PDB entry 5mp4 coloured by chain, side view.
PDB entry 5mp4 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structure, biochemical and kinetic properties of recombinant Pst2p from Saccharomyces cerevisiae, a FMN-dependent NAD(P)H:quinone oxidoreductase.
Koch K, Hromic A, Sorokina M, Strandback E, Reisinger M, Gruber K, Macheroux P
Biochim Biophys Acta Proteins Proteom 1865 1046-1056 (2017)
PMID: 28499769

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171344 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protoplast secreted protein 2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 198 amino acids
Theoretical weight: 20.99 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12335 (Residues: 1-198; Coverage: 100%)
Gene names: D3422, PST2, YD9673.02C, YDR032C
Sequence domains: NADPH-dependent FMN reductase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand PO4 8 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 69.41Å b: 110.56Å c: 223.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.253 0.286
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

MCC/Eisosomes Regulate Cell Wall Synthesis and Stress Responses in Fungi.
Foderaro et al. (2017)
1 more