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3S1V

Transaldolase from Thermoplasma acidophilum in complex with D-fructose 6-phosphate Schiff-base intermediate

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 Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 224
ChainResidue
AASP137
EARG176
EHOH246
AASN170
AILE172
AHIS173
AARG176
AHOH240
EASN170
EILE172
EHIS173

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL B 224
ChainResidue
BASP137
BASN170
BILE172
BHIS173
BARG176
DASN170
DILE172
DHIS173
DARG176
DHOH253

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 225
ChainResidue
AARG176
AVAL179
AILE180
AHOH692

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE F6R C 224
ChainResidue
CASP6
CTHR26
CTHR27
CASN28
CLYS86
CASN108
CTHR110
CSER130
CPHE132
CARG135
CALA166
CSER167
CHOH270
CHOH483
CHOH579
CHOH597

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE F6R A 226
ChainResidue
AASP6
ATHR26
ATHR27
AASN28
ALYS86
AASN108
ATHR110
ASER130
APHE132
AARG135
AALA166
ASER167
AARG169
AHOH245
AHOH247

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE F6R B 225
ChainResidue
BASP6
BTHR26
BTHR27
BASN28
BLYS86
BTHR110
BSER130
BPHE132
BARG135
BALA166
BSER167
BARG169
BHOH253
BHOH267
BHOH683

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE F6R D 224
ChainResidue
DASP6
DTHR27
DASN28
DLYS86
DASN108
DTHR110
DSER130
DPHE132
DARG135
DALA166
DSER167
DARG169
DHOH258
DHOH264
DHOH277

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE F6R E 224
ChainResidue
EHOH760
EASP6
ETHR27
EASN28
ELYS86
ETHR110
ESER130
EPHE132
EARG135
EALA166
ESER167
EARG169
EHOH345
EHOH599

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
DetailsACT_SITE: Schiff-base intermediate with substrate => ECO:0000250
ChainResidueDetails
ALYS86
BLYS86
CLYS86
DLYS86
ELYS86

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PDB entries from 2025-06-11

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