1cdg Summary

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NUCLEOTIDE SEQUENCE AND X-RAY STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 IN A MALTOSE-DEPENDENT CRYSTAL FORM

The structure was published by Lawson, C.L., van Montfort, R., Strokopytov, B., et al., Penninga, D., Dijkhuizen, L., and Dijkstra, B.W., in 1994 in a paper entitled "Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1993.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of CYCLODEXTRIN GLYCOSYL-TRANSFERASE. This molecule has the UniProt identifier P43379 (CDGT2_BACCI)search. The sample contained 686 residues which is 100% of the natural sequence. Out of 686 residues 686 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CYCLODEXTRIN GLYCOSYL-TRANSFERASE P43379 (28-713) (CDGT2_BACCI)search Bacillus circulanssearch 100% 686 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P43379 (28 - 713) CYCLODEXTRIN GLYCOSYL-TRANSFERASE Bacillus circulans

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P43379) E-set domains of sugar-utilizing enzymessearch, Starch-binding domainsearch, alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Glycosidasessearch, Golgi alpha-mannosidase IIsearch, Immunoglobulinssearch PF00128: Alpha amylase, catalytic domainsearch, PF00686: Starch binding domainsearch, PF01833: IPT/TIG domainsearch, PF02806: Alpha amylase, C-terminal all-beta domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P43379) cation bindingsearch catalytic activitysearch starch bindingsearch carbohydrate bindingsearch cyclomaltodextrin glucanotransferase activitysearch transferase activity, transferring glycosyl groupssearch metal ion bindingsearch transferase activitysearch carbohydrate metabolic processsearch extracellular regionsearch

Chain InterPro annotation
A Carbohydrate binding module family 20search IPT domainsearch Alpha amylasesearch Glycosyl hydrolase, family 13, catalytic domainsearch Alpha-amylase, C-terminal all betasearch Glycosyl hydrolase, family 13, subfamily, catalytic domainsearch Glycosyl hydrolase, family 13, all-betasearch Glycoside hydrolase, catalytic domainsearch Immunoglobulin-like foldsearch Carbohydrate-binding-like foldsearch Immunoglobulin E-setsearch Glycoside hydrolase, family 13search Glycoside hydrolase superfamilysearch