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3S1U

Transaldolase from Thermoplasma acidophilum in complex with D-erythrose 4-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004801molecular_functiontransaldolase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006098biological_processpentose-phosphate shunt
A0016740molecular_functiontransferase activity
A0016832molecular_functionaldehyde-lyase activity
B0004801molecular_functiontransaldolase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0006098biological_processpentose-phosphate shunt
B0016740molecular_functiontransferase activity
B0016832molecular_functionaldehyde-lyase activity
C0004801molecular_functiontransaldolase activity
C0005737cellular_componentcytoplasm
C0005975biological_processcarbohydrate metabolic process
C0006098biological_processpentose-phosphate shunt
C0016740molecular_functiontransferase activity
C0016832molecular_functionaldehyde-lyase activity
D0004801molecular_functiontransaldolase activity
D0005737cellular_componentcytoplasm
D0005975biological_processcarbohydrate metabolic process
D0006098biological_processpentose-phosphate shunt
D0016740molecular_functiontransferase activity
D0016832molecular_functionaldehyde-lyase activity
E0004801molecular_functiontransaldolase activity
E0005737cellular_componentcytoplasm
E0005975biological_processcarbohydrate metabolic process
E0006098biological_processpentose-phosphate shunt
E0016740molecular_functiontransferase activity
E0016832molecular_functionaldehyde-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 224
ChainResidue
CASN170
CASN170

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE E4P A 224
ChainResidue
AHOH308
AHOH578
AASP6
AASN28
ALYS86
APHE132
AARG135
ASER167
AARG169

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE E4P C 225
ChainResidue
CASP6
CASN28
CLYS86
CPHE132
CARG135
CALA166
CSER167
CARG169
CHOH276
CHOH304
CHOH320
CHOH595

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE E4P B 224
ChainResidue
BASP6
BASN28
BLYS86
BPHE132
BARG135
BALA166
BSER167
BARG169
BHOH241
BHOH246
BHOH579
BHOH582
BHOH594

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE E4P D 224
ChainResidue
DASP6
DLYS86
DPHE132
DARG135
DSER167
DARG169
DHOH591

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE E4P E 224
ChainResidue
EASP6
ELYS86
EPHE132
EARG135
EALA166
ESER167
EHOH244
EHOH309
EHOH401
EHOH585
EHOH586

Functional Information from PROSITE/UniProt
site_idPS00958
Number of Residues18
DetailsTRANSALDOLASE_2 Transaldolase active site. AvVKIPmTeDGLrAiKtL
ChainResidueDetails
AALA83-LEU100

site_idPS01054
Number of Residues9
DetailsTRANSALDOLASE_1 Transaldolase signature 1. GVTTNPTLI
ChainResidueDetails
AGLY24-ILE32

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsActive site: {"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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