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1T0U

Crystal structure of E.coli uridine phosphorylase at 2.2 A resolution (Type-A Native)

Replaces:  1LGG
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004850molecular_functionuridine phosphorylase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006218biological_processuridine catabolic process
A0006974biological_processDNA damage response
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0009166biological_processnucleotide catabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0030955molecular_functionpotassium ion binding
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0044206biological_processUMP salvage
B0003824molecular_functioncatalytic activity
B0004850molecular_functionuridine phosphorylase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006218biological_processuridine catabolic process
B0006974biological_processDNA damage response
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0009166biological_processnucleotide catabolic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0030955molecular_functionpotassium ion binding
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0044206biological_processUMP salvage
Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. StGIGgPStSIaveEL
ChainResidueDetails
ASER66-LEU81

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 15003451
ChainResidueDetails
AGLU80
AHIS8
AARG223

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 15003451
ChainResidueDetails
BGLU80
BHIS8
BARG223

site_idMCSA1
Number of Residues4
DetailsM-CSA 787
ChainResidueDetails
ALEU9proton acceptor, proton donor
ALEU81electrostatic stabiliser, polar interaction
ATYR169proton acceptor, proton donor
ATHR224electrostatic stabiliser, polar interaction

site_idMCSA2
Number of Residues4
DetailsM-CSA 787
ChainResidueDetails
BLEU9proton acceptor, proton donor
BLEU81electrostatic stabiliser, polar interaction
BTYR169proton acceptor, proton donor
BTHR224electrostatic stabiliser, polar interaction

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PDB entries from 2024-05-01

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