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8CIP

Crystal structure of transketolase from Geobacillus stearothermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
A0016740molecular_functiontransferase activity
A0016744molecular_functiontransketolase or transaldolase activity
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004802molecular_functiontransketolase activity
B0005829cellular_componentcytosol
B0006098biological_processpentose-phosphate shunt
B0016740molecular_functiontransferase activity
B0016744molecular_functiontransketolase or transaldolase activity
B0046872molecular_functionmetal ion binding
C0003824molecular_functioncatalytic activity
C0004802molecular_functiontransketolase activity
C0005829cellular_componentcytosol
C0006098biological_processpentose-phosphate shunt
C0016740molecular_functiontransferase activity
C0016744molecular_functiontransketolase or transaldolase activity
C0046872molecular_functionmetal ion binding
D0003824molecular_functioncatalytic activity
D0004802molecular_functiontransketolase activity
D0005829cellular_componentcytosol
D0006098biological_processpentose-phosphate shunt
D0016740molecular_functiontransferase activity
D0016744molecular_functiontransketolase or transaldolase activity
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00801
Number of Residues21
DetailsTRANSKETOLASE_1 Transketolase signature 1. RtlsIDaiekakSGHPGmpMG
ChainResidueDetails
AARG14-GLY34

site_idPS00802
Number of Residues17
DetailsTRANSKETOLASE_2 Transketolase signature 2. GEDGPTHePIEqlAslR
ChainResidueDetails
AGLY468-ARG484

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P27302
ChainResidueDetails
AGLU412
BGLU412
CGLU412
DGLU412

site_idSWS_FT_FI2
Number of Residues60
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P27302
ChainResidueDetails
AHIS28
ASER385
APHE438
AHIS462
AASP470
AHIS474
AARG521
BHIS28
BHIS68
BGLY116
BASP157
AHIS68
BGLY158
BASN187
BILE189
BHIS263
BARG358
BSER385
BPHE438
BHIS462
BASP470
BHIS474
AGLY116
BARG521
CHIS28
CHIS68
CGLY116
CASP157
CGLY158
CASN187
CILE189
CHIS263
CARG358
AASP157
CSER385
CPHE438
CHIS462
CASP470
CHIS474
CARG521
DHIS28
DHIS68
DGLY116
DASP157
AGLY158
DGLY158
DASN187
DILE189
DHIS263
DARG358
DSER385
DPHE438
DHIS462
DASP470
DHIS474
AASN187
DARG521
AILE189
AHIS263
AARG358

220113

PDB entries from 2024-05-22

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