Domenico:
Both Interproscan and Genthreader support the hypothesis that this target is an alginate lyase, which bind a family of 1-4-linked copolymers of beta-D-mannuronic acid and alpha-L-guluronic acid. The catalytic site is made up of Asn239, Arg289 and Tyr295, which are identically conserved with respect to the template 1qazA0 annotated in CSA.
In principle, other ligand binding residues could be determined from 1hv6, 3afl and 2fut, which are alternative conformations of 1qazA0 and 3a0oA0 and 3e7jA0, respectively, bound to valid ligands. Unfortunately, there's no sequence sonservation or contact consensus, so I would not add anything else.

PFRMAT FN
TARGET T0588
AUTHOR 7656-5034-1890
REMARK Sequence consensus of contacts between homologous structures and ligands
METHOD pGenTHREADER and PDBSum and CSA data mining.
MODEL 1
Binding site: 239, 289, 295
END

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« This page (revision-1) was last changed on 29-Jun-2010 23:30 by UnknownAuthor