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5XU9

Crystal Structure of Transketolase in complex with TPP intermediate IX and gauche form erythrose-4-phosphate from Pichia Stipitis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0006163biological_processpurine nucleotide metabolic process
A0016740molecular_functiontransferase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA A 701
ChainResidue
AASP155
AASN185
AILE187
A8N9709
AHOH870

site_idAC2
Number of Residues3
Detailsbinding site for residue PEG A 702
ChainResidue
AALA134
AASN138
ALYS139

site_idAC3
Number of Residues5
Detailsbinding site for residue PEG A 703
ChainResidue
AHIS211
AILE212
AGLU214
AHOH807
ALYS206

site_idAC4
Number of Residues4
Detailsbinding site for residue PEG A 704
ChainResidue
AGLN526
APRO640
APHE643
AHOH822

site_idAC5
Number of Residues4
Detailsbinding site for residue PEG A 705
ChainResidue
AASN310
APHE313
ALEU331
AASP332

site_idAC6
Number of Residues4
Detailsbinding site for residue PEG A 706
ChainResidue
ATHR198
ALYS206
ASER207
AHOH909

site_idAC7
Number of Residues3
Detailsbinding site for residue PEG A 707
ChainResidue
ALEU645
AHOH808
AHOH1068

site_idAC8
Number of Residues4
Detailsbinding site for residue PEG A 708
ChainResidue
AGLN303
AGLN306
AASN310
AHOH823

site_idAC9
Number of Residues27
Detailsbinding site for residue 8N9 A 709
ChainResidue
AHIS27
AHIS66
AHIS100
AGLY114
APRO115
ALEU116
AASP155
AGLY156
AGLU160
AASN185
AILE187
ASER188
AILE189
AILE248
AHIS261
AASP379
AGLU415
APHE439
APHE442
ATYR445
AHIS478
ACA701
AE4P710
AHOH886
AHOH974
AHOH1098
AHOH1110

site_idAD1
Number of Residues14
Detailsbinding site for residue E4P A 710
ChainResidue
AHIS27
AILE189
AHIS261
AARG356
ALEU380
ASER383
APHE439
AHIS466
AASP474
AARG525
A8N9709
AHOH804
AHOH1010
AHOH1239

Functional Information from PROSITE/UniProt
site_idPS00801
Number of Residues21
DetailsTRANSKETOLASE_1 Transketolase signature 1. RllaVDavaaanSGHPGapLG
ChainResidueDetails
AARG13-GLY33

site_idPS00802
Number of Residues17
DetailsTRANSKETOLASE_2 Transketolase signature 2. GEDGPTHqPIEtlAhfR
ChainResidueDetails
AGLY472-ARG488

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU415

site_idSWS_FT_FI2
Number of Residues15
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS27
ASER383
AGLU415
APHE442
AHIS466
AASP474
AARG525
AHIS66
AGLY114
AASP155
AGLY156
AASN185
AILE187
AHIS261
AARG356

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
AHIS27
AHIS261

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PDB entries from 2024-07-31

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