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4XZ9

Transaldolase variant E60Q/F132Y from T. acidophilum in complex with DHA Schiff base and G3P

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 Residues12
Detailsbinding site for residue GOL A 301
ChainResidue
AASP137
EARG176
EGOL301
EHOH408
AASN170
AILE172
AHIS173
AARG176
AHOH407
EASN170
EILE172
EHIS173

site_idAC2
Number of Residues8
Detailsbinding site for residue G3P B 302
ChainResidue
BASP6
BASN28
BTYR132
BARG135
BSER167
BARG169
BPDO301
BHOH479

site_idAC3
Number of Residues11
Detailsbinding site for residue GOL B 303
ChainResidue
BASN170
BHIS173
BARG176
BHOH407
DASP137
DASN170
DILE172
DHIS173
DARG176
DGOL301
DHOH408

site_idAC4
Number of Residues8
Detailsbinding site for residue ACT B 304
ChainResidue
BARG169
BASN170
BHOH420
BHOH442
BHOH509
DARG169
DASN170
DHOH481

site_idAC5
Number of Residues9
Detailsbinding site for residue G3P C 302
ChainResidue
CASP6
CTYR132
CARG135
CALA166
CSER167
CARG169
CPDO301
CHOH443
CHOH471

site_idAC6
Number of Residues11
Detailsbinding site for residue GOL C 303
ChainResidue
CASP137
CASN170
CASN170
CILE172
CILE172
CHIS173
CHIS173
CARG176
CARG176
CHOH412
CHOH412

site_idAC7
Number of Residues8
Detailsbinding site for residue ACT C 304
ChainResidue
CARG169
CARG169
CASN170
CASN170
CHOH414
CHOH414
CHOH501
CHOH501

site_idAC8
Number of Residues12
Detailsbinding site for residue GOL D 301
ChainResidue
BASP137
BASN170
BILE172
BHIS173
BARG176
BGOL303
BHOH407
DASN170
DILE172
DHIS173
DARG176
DHOH408

site_idAC9
Number of Residues12
Detailsbinding site for residue GOL E 301
ChainResidue
AASN170
AILE172
AHIS173
AARG176
AGOL301
AHOH407
EASP137
EASN170
EILE172
EHIS173
EARG176
EHOH408

site_idAD1
Number of Residues7
Detailsbinding site for residue ACT E 302
ChainResidue
AARG169
AASN170
AHOH424
EARG169
EASN170
EHOH420
EHOH443

site_idAD2
Number of Residues7
Detailsbinding site for residue ACT E 303
ChainResidue
EPHE154
EASN155
EILE158
EILE159
ELYS160
EHOH433
EARG151

site_idAD3
Number of Residues14
Detailsbinding site for Di-peptide PDO B 301 and LYS B 86
ChainResidue
BASP6
BTHR26
BTHR27
BASN28
BVAL59
BGLN60
BVAL61
BVAL84
BVAL85
BILE87
BASN108
BSER130
BG3P302
BHOH405

site_idAD4
Number of Residues14
Detailsbinding site for Di-peptide PDO C 301 and LYS C 86
ChainResidue
CASP6
CTHR26
CTHR27
CASN28
CVAL59
CGLN60
CVAL61
CVAL84
CVAL85
CILE87
CASN108
CSER130
CG3P302
CHOH406

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

224004

PDB entries from 2024-08-21

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