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5XSB

Crystal Structure of Transketolase in complex with TPP intermediate III from Pichia Stipitis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004802molecular_functiontransketolase activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
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
A8EL702
AHOH971

site_idAC2
Number of Residues25
Detailsbinding site for residue 8EL A 702
ChainResidue
ALEU116
AASP155
AGLY156
AGLU160
AASN185
AILE187
ASER188
AILE189
AILE248
AHIS261
AASP379
AGLU415
APHE442
ATYR445
AHIS478
ACA701
AHOH971
AHOH975
AHOH1121
AHOH1147
AHOH1458
AALA30
AHIS66
AGLY114
APRO115

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
AHIS66
AGLY114
AASP155
AGLY156
AASN185
AILE187
AHIS261
AARG356
ASER383
AGLU415
APHE442
AHIS466
AASP474
AARG525
AHIS27

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

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PDB entries from 2024-06-12

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