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1CDG

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0030246molecular_functioncarbohydrate binding
A0043169molecular_functioncation binding
A0043895molecular_functioncyclomaltodextrin glucanotransferase activity
A0046872molecular_functionmetal ion binding
A2001070molecular_functionstarch binding
Functional Information from PDB Data
site_idCA1
Number of Residues6
Details1ST CALCIUM ION BINDING SITE
ChainResidue
AASP27
AASN29
AASN32
AASN33
AGLY51
AASP53

site_idCA2
Number of Residues4
Details2ND CALCIUM ION BINDING SITE
ChainResidue
AASN139
AILE190
AASP199
AHIS233

site_idCAT
Number of Residues3
DetailsCATALYTIC RESIDUE SITE
ChainResidue
AASP229
AGLU257
AASP328

site_idMB1
Number of Residues5
Details1ST MALTOSE BINDING SITE
ChainResidue
ATRP616
ALYS651
ATRP662
AGLU663
AASN667

site_idMB2
Number of Residues7
Details2ND MALTOSE BINDING SITE
ChainResidue
ATHR598
AALA599
AGLY601
AASN603
AASN627
AGLN628
ATYR633

site_idMB3
Number of Residues7
Details3RD MALTOSE BINDING SITE
ChainResidue
ATYR301
AGLU411
AARG412
ATRP413
AILE414
AGLY446
AVAL448

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues81
DetailsDomain: {"description":"IPT/TIG"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues105
DetailsDomain: {"description":"CBM20","evidences":[{"source":"PROSITE-ProRule","id":"PRU00594","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues137
DetailsRegion: {"description":"A1"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues63
DetailsRegion: {"description":"B"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues203
DetailsRegion: {"description":"A2"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues88
DetailsRegion: {"description":"C"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues86
DetailsRegion: {"description":"D"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues103
DetailsRegion: {"description":"E"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 8107143, 10331869, 7493956, 9245426
ChainResidueDetails
AASP328
AGLU257
AASP229
AARG227
AHIS327

site_idMCSA1
Number of Residues5
DetailsM-CSA 45
ChainResidueDetails
AARG227electrostatic stabiliser, hydrogen bond donor
AASP229nucleofuge, nucleophile
AGLU257hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS327electrostatic stabiliser, hydrogen bond donor
AASP328electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2025-08-27

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