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3S1X

Transaldolase from Thermoplasma acidophilum in complex with D-sedoheptulose 7-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 Residues17
DetailsBINDING SITE FOR RESIDUE I22 A 224
ChainResidue
AASP6
ASER167
AARG169
AHOH226
AHOH243
AHOH248
AHOH257
AHOH400
AHOH726
ATHR27
AASN28
ALYS86
ATHR110
ASER130
APHE132
AARG135
AALA166

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE I22 E 224
ChainResidue
EASP6
ETHR27
EASN28
ELYS86
ETHR110
ESER130
EPHE132
EARG135
EALA166
ESER167
EARG169
EHOH245
EHOH250
EHOH252
EHOH253
EHOH272
EHOH633

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE I22 D 224
ChainResidue
DASP6
DTHR27
DASN28
DLYS86
DASN108
DTHR110
DSER130
DPHE132
DARG135
DALA166
DSER167
DARG169
DHOH239
DHOH240
DHOH246
DHOH266
DHOH323
DHOH873

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE I22 C 224
ChainResidue
CASP6
CTHR26
CTHR27
CASN28
CLYS86
CASN108
CTHR110
CSER130
CPHE132
CARG135
CALA166
CSER167
CARG169
CHOH237
CHOH255
CHOH273
CHOH360
CHOH378
CHOH1183

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE I22 B 224
ChainResidue
BASP6
BTHR26
BTHR27
BASN28
BLYS86
BASN108
BTHR110
BSER130
BPHE132
BARG135
BALA166
BSER167
BARG169
BHOH235
BHOH240
BHOH254
BHOH354
BHOH567
BHOH721

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

237992

PDB entries from 2025-06-25

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