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5XRY

Crystal Structure of Transketolase contains cysteinesufonic acid 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 Residues6
Detailsbinding site for residue CA A 701
ChainResidue
AASP155
AASN185
AILE187
AHOH899
AHOH1124
AHOH1214

site_idAC2
Number of Residues2
Detailsbinding site for residue PEG A 702
ChainResidue
AALA134
AASN138

site_idAC3
Number of Residues2
Detailsbinding site for residue PEG A 703
ChainResidue
AGLN328
AASN310

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

238895

PDB entries from 2025-07-16

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