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4RZ6

Transaldolase B E96Q F178Y from E.coli

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 PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AARG181
ASER226
AARG228
AHOH573

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AHOH602
AARG92
APHE173
AARG241
AHOH538
AHOH540

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE P6G A 403
ChainResidue
ATRP137
AGLN138
AGLU278
APHE281
ALEU282
AHIS285
AASN286
ACL404
AHOH578
BTYR103
BTRP137
BGLN138
BGLU278
BPHE281
BLEU282

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 404
ChainResidue
AASN286
AP6G403
BTYR103
BLEU295
BHOH518

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
BARG92
BPHE173
BARG241
BHOH516
BHOH550
BHOH568
BHOH662

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 402
ChainResidue
BARG181
BSER226
BARG228
BHOH595

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 403
ChainResidue
AASN286
AHOH504
BTYR103
BALA296
BILE299

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 404
ChainResidue
BVAL97
BSER102
BSER108
BHOH501
BHOH517

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 405
ChainResidue
BALA110
BLYS111
BHOH502
BHOH561
BHOH633

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
DetailsActive site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"11298760","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 148
ChainResidueDetails
AASP17hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLN96electrostatic 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
ATYR178steric role

site_idMCSA2
Number of Residues5
DetailsM-CSA 148
ChainResidueDetails
BASP17hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLN96electrostatic 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
BTYR178steric role

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PDB entries from 2026-01-21

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