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Structure paper

TitleA potential substrate binding pocket of BdcA plays a critical role in NADPH recognition and biofilm dispersal
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 497, Page 863-868, Year 2018
Publish dateJan 3, 2018 (structure data deposition date)
AuthorsYang, W.S. / Hong, Y. / Zhang, Y. / Wang, D.C. / Li, D.F. / Hou, Y.J.
External linksBiochem. Biophys. Res. Commun. / PubMed:29462616
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-5z2l:
Crystal structure of BdcA in complex with NADPH
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-PG0:
2-(2-METHOXYETHOXY)ETHANOL / inhibitor, precipitant*YM

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
KeywordsOXIDOREDUCTASE / short-chain dehydrogenase/reductase (SDR) / NADPH binding / biofilm dispersal

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