148 GAL GLC CAT_SITE
253 GAL GLC CAT_SITE

Domenico:
This target is unlikely to be an aldose 1-epimerase, despite Interproscan results. Swissprot entry for this E.coli K12 enzime is P0A9C3. The target probably evolved from gene duplication - which would support the loss of Asp in the catalytic triad and its substitution with Asn. Regardless of the divergence of molecular function, the binding region could well be conserved, and so we could use a revised version of our protocol anyway. In this specific case I would just discard information from CSA. Unfortunately, this strategy only leaves three valid protein-lingand intercations to analyze. The consensus prediction includes Asp44, Arg56, Tyr81, His148, Tyr150, Asn200, Phe235 and Glu253. All these residues cluster altogether in the manual 3D model.

PFRMAT FN
TARGET T0526
AUTHOR 7656-5034-1890
REMARK Sequence consensus of contacts between homologous structures and ligands
METHOD pGenTHREADER and PDBSum data mining.
MODEL 1
Binding site: 44, 56, 81, 148, 150, 200, 235, 253
END

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« This page (revision-1) was last changed on 28-May-2010 17:18 by UnknownAuthor