This target likely belongs to the short-chain dehydrogenases/reductases family. The consensus from CSA data includes Asn117, Ser145, Gly155, Tyr158 and Lys162. However, Gly155 is not part of the catalytic site entry for this class of enzymes, so i'd discard it.
These enzymes bind need NAD or NADH to carrry out their function. At least 10 out of 21 valid nucleotide-template interactions support the hypothesis that these residues form an equivalent binding site: Gly14, Ser16, Gln17, Gly18, Ile19, Ala38, Arg39, Ser40, Leu66, Asp67, Ile68, Ala94, Ala95, Ala96, Met97, Ile116, Val 143, Ala144, Ser145, Tyr158, Lys162, Pro188, Gly189, Trp190, Val191, Thr193, Asp194, Met195 and Ala195.
Unfortunately, only four templates were complecxed with a valid substrate. Residues Phe98, Ser145, Gly155, Tyr158 and Met195 come from the consensus of at least 3 out of 4 homologs.

AUTHOR 7656-5034-1890
REMARK Sequence consensus of contacts between homologous structures and ligands
METHOD pGenTHREADER and PDBSum and CSA data mining.
Binding site: 14, 16, 17, 18, 19, 38, 39, 40, 66, 67, 68, 94, 95, 96, 97, 98, 116, 117, 143, 144, 145, 155, 158, 162, 188, 189, 190, 191, 193, 194, 195, 195

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« This page (revision-1) was last changed on 27-Jul-2010 14:31 by UnknownAuthor