Interproscan predicts that this target is a FAD dependent oxidoreductase, which agrees with the nature of ligands complexed with Genthreader's hits. Unfortunately CSA annotations are not reliable in this case, as the templates were already annotated by homology and potential catalytic sites are not conserved. Ion contacts do not cluster not even for the same chemical element, so they are unlikely to be relevant from a biological standpoint. The following residues are found in contact with NAD or analogous molecules in at least 11 out of 32 complexes: Ile113, Gly114, Phe115, Gly116, Pro117, Cys118, Val136, Glu137, Arg138, Gly139, Glu144, Arg145, Thr146, Asp148, Thr149, Phe150, Thr241, Arg242, Val243, Ala272, Val273, Gly274, Gly515, Glu516, Gly523 and Ile524. Other valid ligands do not appear to prefer binding to particular regions, which could reflect the diversity of processes involving oxidoreductases.

AUTHOR 7656-5034-1890
REMARK Sequence consensus of contacts between homologous structures and ligands
METHOD pGenTHREADER and PDBSum and CSA data mining.
Binding site: 113, 114, 115, 116, 117, 118, 136, 137, 138, 139, 144, 145, 146, 148, 149, 150, 241, 242, 243, 272, 273, 274, 515, 516, 523, 524

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