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1TPT

THREE-DIMENSIONAL STRUCTURE OF THYMIDINE PHOSPHORYLASE FROM ESCHERICHIA COLI AT 2.8 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0005829cellular_componentcytosol
A0006206biological_processpyrimidine nucleobase metabolic process
A0006213biological_processpyrimidine nucleoside metabolic process
A0006974biological_processDNA damage response
A0009032molecular_functionthymidine phosphorylase activity
A0016020cellular_componentmembrane
A0016154molecular_functionpyrimidine-nucleoside phosphorylase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046104biological_processthymidine metabolic process
Functional Information from PDB Data
site_idSO4
Number of Residues6
DetailsSULFATE BINDING SITE
ChainResidue
ALYS84
AHIS85
ASER86
ASER95
ASER113
ATHR123

site_idTDR
Number of Residues3
DetailsTHYMINE BINDING SITE
ChainResidue
AARG171
ASER186
ALYS190

Functional Information from PROSITE/UniProt
site_idPS00647
Number of Residues16
DetailsTHYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SGRGLghTGGTlDkLE
ChainResidueDetails
ASER113-GLU128

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1azy
ChainResidueDetails
AHIS85
AARG171
ALYS190

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1azy
ChainResidueDetails
AHIS85
ASER186
AARG171
ALYS190

site_idMCSA1
Number of Residues9
DetailsM-CSA 413
ChainResidueDetails
AASP83proton shuttle (general acid/base)
ALYS84activator, electrostatic stabiliser
AHIS85electrostatic stabiliser
ASER86electrostatic stabiliser
ATHR123electrostatic stabiliser
AARG171electrostatic stabiliser
ASER186electrostatic stabiliser
ALYS190electrostatic stabiliser, proton shuttle (general acid/base)
ALYS191electrostatic stabiliser

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PDB entries from 2024-07-10

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