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1A47

CGTASE FROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR

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_idAM1
Number of Residues3
DetailsSUGAR BINDING SUBSITE -1 IN THE ACTIVE SITE.
ChainResidue
CG6D3
AHIS234
AGLU258

site_idAM2
Number of Residues4
DetailsSUGAR BINDING SUBSITE -2 IN THE ACTIVE SITE.
ChainResidue
CGLC2
ALYS233
APHE184
APHE260

site_idAM3
Number of Residues4
DetailsSUGAR BINDING SUBSITE -3 IN THE ACTIVE SITE.
ChainResidue
CGLC1
AGLU265
ATHR263
AASN591

site_idAP1
Number of Residues8
DetailsSUGAR BINDING SUBSITE +1 IN THE ACTIVE SITE (CATALYTIC SITE).
ChainResidue
AADH694
ATYR101
AHIS141
AARG228
AASP230
AGLU258
AHIS328
AASP329

site_idAP2
Number of Residues4
DetailsSUGAR BINDING SUBSITE +2 IN THE ACTIVE SITE.
ChainResidue
DGLC1
ATRP102
AASP371
AARG375

site_idAP3
Number of Residues2
DetailsSUGAR BINDING SUBSITE +3 IN THE ACTIVE SITE.
ChainResidue
DGLC2
ALYS47

site_idBS3
Number of Residues7
DetailsSUGAR BINDING SITE 3 (HOMOLOGOUS TO MBS3 IN PDB ENTRY 1CDG).
ChainResidue
BGLC1
BGLC2
BGLC3
ATRP413
AGLN411
AILE414
AGLY446

site_idCA1
Number of Residues6
DetailsCALCIUM BINDING SITE.
ChainResidue
AASP27
AASN29
AASN32
AASN33
AGLY51
AASP53

site_idCA2
Number of Residues4
DetailsCALCIUM BINDING SITE.
ChainResidue
AHIS234
AASN140
AILE191
AASP200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:8604143
ChainResidueDetails
AASP230

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:8604143
ChainResidueDetails
AGLU258

site_idSWS_FT_FI3
Number of Residues14
DetailsBINDING:
ChainResidueDetails
AASP27
AASP200
ALYS233
AHIS234
AASP371
AARG375
AASN29
AASN32
AASN33
AGLY51
AASP53
ATYR101
AASN140
AILE191

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS141
AASN194
AARG228
AHIS328

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASP329

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
ATHR255
AASP230

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLN292
AASP371
AASP230

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AHIS328
AARG228
AASP329
AGLU258
AASP230

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AGLU258
AASP230

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AHIS141
AASP329
AGLU258
AASP230

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP329
AGLU258
AASP230

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP320
AGLU258
AASP230

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1amy
ChainResidueDetails
AASP329
AGLU258
APHE260
AASP230

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PDB entries from 2024-09-04

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