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1UKQ

Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose

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
B0003824molecular_functioncatalytic activity
B0004556molecular_functionalpha-amylase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0016757molecular_functionglycosyltransferase activity
B0030246molecular_functioncarbohydrate binding
B0043169molecular_functioncation binding
B0043895molecular_functioncyclomaltodextrin glucanotransferase activity
B0046872molecular_functionmetal ion binding
B2001070molecular_functionstarch binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
AASP229
BASP229

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AGLU257
BGLU257

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING:
ChainResidueDetails
AASP27
AASN193
AASP199
AHIS233
AASP371
AARG375
BASP27
BASN29
BASN32
BASN33
BGLY51
AASN29
BASP53
BTYR100
BASN139
BILE190
BASN193
BASP199
BHIS233
BASP371
BARG375
AASN32
AASN33
AGLY51
AASP53
ATYR100
AASN139
AILE190

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS140
AARG227
ALYS232
AHIS327
BHIS140
BARG227
BLYS232
BHIS327

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP328
BASP328

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

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP328
BASP229
BGLU257

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU264
AASP328
AASP229

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BGLU264
BASP328
BASP229

site_idCSA13
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
APHE259
AASP328
AASP229
AGLU257

site_idCSA14
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BPHE259
BASP328
BASP229
BGLU257

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BTHR254
BASP229

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AGLU257
AASP229
AARG227
AHIS327

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP328
BGLU257
BASP229
BARG227
BHIS327

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP229
AGLU257

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP229
BGLU257

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AGLU257
AASP229
AHIS140

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
BASP328
BGLU257
BASP229
BHIS140

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP328
AASP229
AGLU257

222036

PDB entries from 2024-07-03

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