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1RXY

E. coli uridine phosphorylase: type-B native

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
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 1001
ChainResidue
AGLU49
AILE69
ASER73
BGLU49
BILE69
BSER73

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 4001
ChainResidue
AHIS8
AGLY10
ASER4
AVAL6
APHE7

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 6001
ChainResidue
AARG48
AHOH6147
AHOH6148
AHOH6149
BGLY26
BARG91
BHOH3171

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 2001
ChainResidue
AARG115
ALEU116
ALEU121
ALEU126
AHOH6020
AHOH6021
AHOH6094
AHOH6104
AHOH6135

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 3001
ChainResidue
BARG115
BLEU116
BLEU126
BHIS179
BHOH3031
BHOH3034
BHOH3129
BHOH3142
BHOH3143

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 5001
ChainResidue
ATHR111
AALA132
ATHR137
BTHR111
BALA132
BTHR137

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
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 2024-07-31

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