1dav

SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (20 STRUCTURES)SOLUTION STRUCTURE OF THE TYPE I DOCKERIN DOMAIN FROM THE CLOSTRIDIUM THERMOCELLUM CELLULOSOME (20 STRUCTURES)

Structural highlights

1dav is a 1 chain structure with sequence from Acetivibrio thermocellus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUNS_ACETH This enzyme catalyzes the exohydrolysis of 1,4-beta-glucosidic linkages in cellulose with a preference for amorphous or crystalline cellulose over carboxymethyl cellulose.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Saharay M, Guo H, Smith JC. Catalytic mechanism of cellulose degradation by a cellobiohydrolase, CelS. PLoS One. 2010 Oct 12;5(10):e12947. PMID:20967294 doi:10.1371/journal.pone.0012947

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Saharay M, Guo H, Smith JC. Catalytic mechanism of cellulose degradation by a cellobiohydrolase, CelS. PLoS One. 2010 Oct 12;5(10):e12947. PMID:20967294 doi:10.1371/journal.pone.0012947

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