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Structure paper

TitleRole of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site
Journal, issue, pagesPROTEIN SCI., Vol. 13, Page 457-465, Year 2004
Publish dateNov 3, 2003 (structure data deposition date)
AuthorsKanai, R. / Haga, K. / Akiba, T. / Yamane, K. / Harata, K.
External linksPROTEIN SCI. / PubMed:14739329
MethodsX-ray diffraction
Resolution2 - 2.1 Å
Structure data

PDB-1v3j:
Crystal structure of F283L mutant cyclodextrin glycosyltransferase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1v3k:
Crystal structure of F283Y mutant cyclodextrin glycosyltransferase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1v3l:
Crystal structure of F283L mutant cyclodextrin glycosyltransferase complexed with a pseudo-tetraose derived from acarbose
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1v3m:
Crystal structure of F283Y mutant cyclodextrin glycosyltransferase complexed with a pseudo-tetraose derived from acarbose
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GLC:
alpha-D-glucopyranose

ChemComp-ACI:
6-AMINO-4-HYDROXYMETHYL-CYCLOHEX-4-ENE-1,2,3-TRIOL

ChemComp-GAL:
beta-D-galactopyranose

Source
  • bacillus sp. (bacteria)
KeywordsTRANSFERASE / CGTASE / CYCLODEXTRIN / Acarbose

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