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1I2R

CRYSTAL STRUCTURE OF ESCHERICHIA COLI TRANSALDOLASE B MUTANT S176A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004801molecular_functiontransaldolase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006098biological_processpentose-phosphate shunt
A0009052biological_processpentose-phosphate shunt, non-oxidative branch
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016744molecular_functiontransketolase or transaldolase activity
B0004801molecular_functiontransaldolase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006098biological_processpentose-phosphate shunt
B0009052biological_processpentose-phosphate shunt, non-oxidative branch
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016744molecular_functiontransketolase or transaldolase activity
Functional Information from PROSITE/UniProt
site_idPS00958
Number of Residues18
DetailsTRANSALDOLASE_2 Transaldolase active site. IlIKLAsTwQGIrAaEqL
ChainResidueDetails
AILE129-LEU146

site_idPS01054
Number of Residues9
DetailsTRANSALDOLASE_1 Transaldolase signature 1. DATTNPSLI
ChainResidueDetails
AASP31-ILE39

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000269|PubMed:11298760
ChainResidueDetails
ALEU133
BLEU133

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
AASP17
AGLU96
ALYS132

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1onr
ChainResidueDetails
BASP17
BGLU96
BLYS132

site_idMCSA1
Number of Residues5
DetailsM-CSA 148
ChainResidueDetails
AASP17hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU96electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS132covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ATHR156electrostatic stabiliser, hydrogen bond donor
APHE178steric role

site_idMCSA2
Number of Residues5
DetailsM-CSA 148
ChainResidueDetails
BASP17hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLU96electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BLYS132covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BTHR156electrostatic stabiliser, hydrogen bond donor
BPHE178steric role

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PDB entries from 2025-06-18

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