Uniprot annotation defines the catalytic activiy of this protein and suggests that the triads Asp171-Asp358-His359 and Asp311-His315-His474 are involved in binding divalent metal cations. Not surprisingly, none of Genthreader's hits is bound to lysophospholipids - the major substrates. According to MOAD contacts between vanadate and the closest template 2gsoA0 are not valid. However, vanadate is a potent inhibitor of enzymes that catalyze phosphoryl transfer reactions and adopts a trigonal bipyramidal geometry analogous to the transition state for phosphate ester hydrolysis. This means we could use those contacts to infer the location of the catalytic site. Beisdes, the same template has been complexed with AMP - which is analogous to the nucleoside product of hydrolysis - and we could make use of that structure too. Indeed, the target can hydrolyze ATP as well. Contacts between different templates with Zinc or Calcium are in agreement with Uniprot, although it might be somewhat circular. Binding residues inferred from 2gsoA0-vanadate: Asp171, Lys208, Thr209, Asn230, His242, Asp311, His315, Hist359, Gln471
Binding residues inferred from 2gsu-AMP: Thr209, Phe210, Asn230, His242, Tyr306, Glu308, Asp311, His315, His474
Intersection of these two sets: Thr209, Asn230, His242, Asp311, His315

AUTHOR 7656-5034-1890
REMARK Sequence consensus of contacts between homologous structures and ligands
METHOD pGenTHREADER and PDBSum and CSA data mining.
Binding site: 171, 209, 230, 242, 311, 315, 358, 359, 474

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« This page (revision-1) was last changed on 16-Jun-2010 11:09 by UnknownAuthor