› 1sny

X-ray diffraction
1.75Å resolution

Carbonyl reductase Sniffer of D. melanogaster

Released:
DOI: 10.2210/pdb1sny/pdb
PDB entry 1sny coloured by chain, front view.
PDB entry 1sny coloured by chain, side view.
PDB entry 1sny coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Structural insights into the neuroprotective-acting carbonyl reductase Sniffer of Drosophila melanogaster.
Sgraja T, Ulschmid J, Becker K, Schneuwly S, Klebe G, Reuter K, Heine A
J. Mol. Biol. 342 1613-24 (2004)
PMID: 15364585

Function and Biology Details

Reaction catalysed: 
R-CHOH-R' + NADP(+) = R-CO-R' + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194338 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sniffer, isoform A Chain: A
Molecule details ›
Chain: A
Length: 267 amino acids
Theoretical weight: 29.04 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9W3H4 (Residues: 1-247; Coverage: 100%)
Gene names: CG10964, Dmel\CG10964, Dmel_CG10964, SNI, Sni, anon-WO03040301.183, sni
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
No bound ligands
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: I222
Unit cell:
a: 71.7Å b: 73.9Å c: 92.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.247 0.284
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology.
Oppermann U. (2007)
2 more

2 mentions without citation

Assisted assignment of ligands corresponding to unknown electron density.
Binkowski et al. (2010)
1 more