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1CGW

SITE DIRECTED MUTATIONS OF THE ACTIVE SITE RESIDUE TYROSINE 195 OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 AFFECTING ACTIVITY AND PRODUCT SPECIFICITY

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004556molecular_functionalpha-amylase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
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 BINDING SITE
ChainResidue
AASP27
AASN29
AASN32
AASN33
AGLY51
AASP53

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

site_idCAT
Number of Residues3
DetailsCATALYTIC SITE
ChainResidue
AASP229
AGLU257
AASP328

site_idMB1
Number of Residues5
DetailsFIRST 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 Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP229

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU257

site_idSWS_FT_FI3
Number of Residues21
DetailsBINDING:
ChainResidueDetails
AASP27
ASER145
AILE190
AASN193
AASP199
AARG227
ALYS232
AHIS233
AALA315
AHIS327
AASP371
AASN29
AARG375
AASP577
AASN32
AASN33
AGLY51
AASP53
ATYR100
AASN139
AHIS140

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP328

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
ATHR254
AASP229

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AGLU257
AASP229
AARG227
AHIS327

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP229
AGLU257

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AGLU257
AASP229
AHIS140

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AASP229
AGLU257

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU264
AASP229
AASP319

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
APHE259
AASP328
AASP229
AGLU257

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 2024-10-30

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