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Structure paper

TitleCrystal structures and inhibition of the beta-aminopeptidase BapA, a new ampicillin-recognizing member of the N-terminal nucleophile hydrolase family
Journal, issue, pagesTo be Published
Publish dateJun 8, 2010 (structure data deposition date)
AuthorsHeck, T. / Merz, T. / Geueke, B. / Gruetter, M.G. / Kohler, H.-P.E.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-3ndv:
Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with ampicillin
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-AIC:
(2S,5R,6R)-6-{[(2R)-2-AMINO-2-PHENYLETHANOYL]AMINO}-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC / antibiotic*YM

ChemComp-NDV:
(2S,4S)-2-[(1R)-1-{[(2R)-2-amino-2-phenylacetyl]amino}-2-oxoethyl]-5,5-dimethyl-1,3-thiazolidine-4-carboxylic acid

ChemComp-HOH:
WATER

Source
  • sphingosinicella xenopeptidilytica (bacteria)
KeywordsHYDROLASE/ANTIBIOTIC / Ntn-hydrolase / beta-aminopeptidase / beta-peptide / alpha-beta-beta-alpha sandwich / N-terminal beta-aminopeptidase / HYDROLASE-ANTIBIOTIC complex

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