Brand  (β version)

PDB ID: 1D3C

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
CA Calcium ion PoSSuM
MPD (4s)-2-methyl-2,4-pentanediol PoSSuM
GLC Alpha-D-glucopyranose PoSSuM
: Polysaccharide
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1D3C   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN
Release Data : 1999-12-22
Compound :
mol_id molecule chains
1 CYCLODEXTRIN GLYCOSYLTRANSFERASE A
ec: 2.4.1.19
mutation: D229N, E257Q
Source :
mol_id organism_scientific expression_system
1 Bacillus circulans  (taxid:1397) Bacillus subtilis  (taxid:1423)
strain: 251
cellular_location: EXTRACELLULAR
expression_system_plasmid: PDP66S
Authors : Uitdehaag, J.C.M., Kalk, K.H., van der Veen, B.A., Dijkhuizen, L., Dijkstra, B.W.
Keywords : ALPHA-AMYLASE, PRODUCT COMPLEX, OLIGOSACCHARIDE, FAMILY 13 GLYCOSYL HYDROLASE, TRANSGLYCOSYLATION, INDUCED FIT, CATALYSIS, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.78 Å )
Citation :

The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution.

Uitdehaag, J.C.,Kalk, K.H.,van Der Veen, B.A.  et al.
(1999)  J.Biol.Chem.  274 : 34868 - 34876

PubMed: 10574960
DOI: 10.1074/jbc.274.49.34868

X-ray Structures Along the Reaction Pathway of Cyclodextrin Glycosyltransferase Elucidate Catalysis in the Alpha-amylase Family

Uitdehaag, J.C.M.,Mosi, R.,Kalk, K.H.  et al.
(1999)  Nat.Struct.Biol.  6 : 432 - 436

DOI: 10.1038/8235

Crystallographic Studies of the Interaction of Cyclodextrin Glycosyltransferase from Bacillus Circulans Strain 251 with Natural Substrates and Products

Knegtel, R.M.,Strokopytov, B.,Penninga, D.  et al.
(1995)  J.Biol.Chem.  270 : 29256 - 29264

DOI: 10.1074/jbc.270.49.29256

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 - 4249

DOI: 10.1021/bi952339h

Reaction

Chain : A
UniProt : P43379 (CDGT2_NIACI)
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 PubMed:7493956
-