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4NY1

X-ray structure of the unliganded uridine phosphorylase from Yersinia pseudotuberculosis at 1.7 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004850molecular_functionuridine phosphorylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0009166biological_processnucleotide catabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0044206biological_processUMP salvage
B0003824molecular_functioncatalytic activity
B0004850molecular_functionuridine phosphorylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0009166biological_processnucleotide catabolic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0044206biological_processUMP salvage
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
AGLU49
AILE69
ASER73
BGLU49
BILE69
BSER73

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AHOH562
AARG87
AHOH421
AHOH548

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AASP133
AHOH411
AHOH412
AHOH427

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AGLY105
ATHR237
AHIS240
AHOH540

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEG A 305
ChainResidue
APHE172
ASER189
BGLN209
BGLY210
BTHR224
BGLN225

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 301
ChainResidue
AARG48
BARG91
BGLY93
BTHR94
BGLU198
BHOH612

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. StGIGgPStSIaveEL
ChainResidueDetails
ASER66-LEU81

245663

PDB entries from 2025-12-03

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