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3EUE

Crystal structure of ligand-free human uridine phosphorylase 1 (hUPP1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004850molecular_functionuridine phosphorylase activity
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006218biological_processuridine catabolic process
A0006220biological_processpyrimidine nucleotide metabolic process
A0006248biological_processCMP catabolic process
A0006249biological_processdCMP catabolic process
A0009032molecular_functionthymidine phosphorylase activity
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0009166biological_processnucleotide catabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0042149biological_processcellular response to glucose starvation
A0042802molecular_functionidentical protein binding
A0044206biological_processUMP salvage
A0046050biological_processUMP catabolic process
A0046074biological_processdTMP catabolic process
A0046079biological_processdUMP catabolic process
A0046108biological_processuridine metabolic process
A0047847molecular_functiondeoxyuridine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 311
ChainResidue
ASER116
AILE117
AHIS120
AASP212
APHE213
ATYR214

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 312
ChainResidue
AHOH399
AHOH424
AHOH436
AGLY60
ASER61
AARG64

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. ShGMGiPSiSImlhEL
ChainResidueDetails
ASER107-LEU122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19291308, ECO:0007744|PDB:3EUF
ChainResidueDetails
AGLY60
AARG94
AARG138

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:20856879, ECO:0007744|PDB:3EUF, ECO:0007744|PDB:3NBQ
ChainResidueDetails
ASER142

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:19291308, ECO:0000305|PubMed:20856879, ECO:0007744|PDB:3EUF, ECO:0007744|PDB:3NBQ
ChainResidueDetails
AGLN217

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1t0u
ChainResidueDetails
AGLU121
AARG275
AHIS36

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PDB entries from 2024-07-24

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