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1TGV

Structure of E. coli Uridine Phosphorylase complexed with 5-Fluorouridine and sulfate

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
A0046050biological_processUMP catabolic process
A0047847molecular_functiondeoxyuridine phosphorylase activity
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
B0046050biological_processUMP catabolic process
B0047847molecular_functiondeoxyuridine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 482
ChainResidue
AGLY26
AARG30
AARG91
AILE92
AGLY93
ATHR94
A5UD3001
BARG48

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 682
ChainResidue
BGLY26
BARG30
BARG91
BILE92
BGLY93
BTHR94
B5UD5002
AARG48

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 1001
ChainResidue
AGLU49
AILE69
ASER73
BGLU49
BILE69
BSER73

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 5UD A 3001
ChainResidue
AARG91
ATHR94
ATHR95
AGLY96
APHE162
AGLN166
AARG168
AGLU196
AMET197
AGLU198
AILE220
AVAL221
ASO4482
AHOH3032
AHOH3035
BPHE7
BHIS8

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 5UD B 5002
ChainResidue
AHIS8
BILE69
BARG91
BTHR94
BTHR95
BGLY96
BPHE162
BGLN166
BARG168
BGLU196
BMET197
BGLU198
BILE220
BVAL221
BSO4682
BHOH5020
BHOH5084

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
DetailsAnnotated By Reference To The Literature 1t0u
ChainResidueDetails
AGLU80
AHIS8
AARG223

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1t0u
ChainResidueDetails
BGLU80
BHIS8
BARG223

site_idMCSA1
Number of Residues4
DetailsM-CSA 787
ChainResidueDetails
AHIS8proton acceptor, proton donor
AGLU80electrostatic stabiliser, polar interaction
AARG168proton acceptor, proton donor
AARG223electrostatic stabiliser, polar interaction

site_idMCSA2
Number of Residues4
DetailsM-CSA 787
ChainResidueDetails
BHIS8proton acceptor, proton donor
BGLU80electrostatic stabiliser, polar interaction
BARG168proton acceptor, proton donor
BARG223electrostatic stabiliser, polar interaction

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PDB entries from 2024-09-18

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