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Structure paper

TitleMutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 34665-34676, Year 2010
Publish dateAug 12, 2010 (structure data deposition date)
AuthorsSu, X. / Agarwal, V. / Dodd, D. / Bae, B. / Mackie, R.I. / Nair, S.K. / Cann, I.K.
External linksJ. Biol. Chem. / PubMed:20739280
MethodsX-ray diffraction
Resolution1.35 - 1.55 Å
Structure data

PDB-3oea:
Crystal structure of the Q121E mutants of C.polysaccharolyticus CBM16-1 bound to cellopentaose
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

PDB-3oeb:
Crystal structure of the Q121E mutant of C.polysaccharolyticus CBM16-1 bound to mannopentaose
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • caldanaerobius polysaccharolyticus (bacteria)
KeywordsHYDROLASE / Carbohydrate Binding Domain / Cellopentaose / Family 16 CBM-1 / Carbohydrate Binding Module / Mannopentaose

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