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Ligands
Code Name Style Show Link
ADH 1-amino-2,3-dihydroxy-5-hydroxymethyl cyclohex-5-ene
CA Calcium ion
G6D Alpha-D-quinovopyranose
GLC Alpha-D-glucopyranose
: Polysaccharide
Non-standard Residues
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Glycosylation
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Code : 1A47   PDBj   RCSB PDB   PDBe
Header : GLYCOSIDASE
Title : CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR
Release Data : 1998-06-17
Compound :
mol_id molecule chains synonym
1 CYCLODEXTRIN GLYCOSYLTRANSFERASE A CGTASE
ec: 2.4.1.19
Source :
mol_id organism_scientific expression_system
1 Thermoanaerobacterium thermosulfurigenes  (taxid:33950) Escherichia coli  (taxid:562)
strain: EM1
cellular_location: EXTRACELLULAR
gene: AMYA
expression_system_strain: PC1990
expression_system_cellular_location: EXTRACELLULAR
expression_system_plasmid: PCT2
expression_system_gene: AMYA
Authors : Uitdehaag, J.C.M., Kalk, K.H., Rozeboom, H.J., Dijkstra, B.W.
Keywords : GLYCOSIDASE, THERMOSTABLE, FAMILY 13 GLYCOSYL HYDROLASE, LIGAND, SUBSTRATE, ACARBOSE
Exp. method : X-RAY DIFFRACTION ( 2.56 Å )
Citation :

Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.

Wind, R.D.,Uitdehaag, J.C.,Buitelaar, R.M.  et al.
(1998)  J.Biol.Chem.  273 : 5771 - 5779

PubMed: 9488711
DOI: 10.1074/jbc.273.10.5771

Crystal Structure at 2.3 A Resolution and Revised Nucleotide Sequence of the Thermostable Cyclodextrin Glycosyltransferase from Thermoanaerobacterium Thermosulfurigenes Em1

Knegtel, R.M.,Wind, R.D.,Rozeboom, H.J.  et al.
(1996)  J.Mol.Biol.  256 : 611

Structure of Cyclodextrin Glycosyltransferase Complexed with a Maltononaose Inhibitor at 2.6 Angstrom Resolution. Implications for Product Specificity

Strokopytov, B.,Knegtel, R.M.,Penninga, D.  et al.
(1996)  Biochemistry  35 : 4241

Chain : A
UniProt : P26827 (CDGT_THETU)
Reaction: EC: Evidence:
Physiological Direction:
Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond. 2.4.1.19 -
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