Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5XSA

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004802molecular_functiontransketolase activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006098biological_processpentose-phosphate shunt
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
AHOH998

site_idAC2
Number of Residues23
Detailsbinding site for residue 8EL A 702
ChainResidue
AASP155
AGLY156
AGLU160
AASN185
AILE187
ASER188
AILE189
AILE248
AHIS261
AASP379
AGLU415
APHE442
ATYR445
AHIS478
ACA701
AHOH958
AHOH998
AHOH1053
AHOH1134
AHIS66
AGLY114
APRO115
ALEU116

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
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon