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Structure paper

TitleA hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with wiskott-Aldrich syndrome protein.
Journal, issue, pagesJ. Biol. Chem., Vol. 282, Page 14309-14315, Year 2007
Publish dateFeb 7, 2007 (structure data deposition date)
AuthorsSt-Jean, M. / Izard, T. / Sygusch, J.
External linksJ. Biol. Chem. / PubMed:17329259
MethodsX-ray diffraction
Resolution2.05 Å
Structure data

PDB-2ot0:
Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with a C-terminal peptide of Wiskott-Aldrich syndrome protein
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-2ot1:
Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with naphthol AS-E phosphate, a competitive inhibitor
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-N3P:
N-(4-CHLOROPHENYL)-3-(PHOSPHONOOXY)NAPHTHALENE-2-CARBOXAMIDE

Source
  • oryctolagus cuniculus (rabbit)
KeywordsLYASE / complex / glycolysis / actin dynamics / hydrophobic pocket / WASp / competitive inhibition

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