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3P0F

Structure of hUPP2 in an inactive conformation with bound 5-benzylacyclouridine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004850molecular_functionuridine phosphorylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006218biological_processuridine catabolic process
A0006249biological_processdCMP catabolic process
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0009166biological_processnucleotide catabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0042802molecular_functionidentical protein binding
A0044206biological_processUMP salvage
A0045098cellular_componenttype III intermediate filament
A0046108biological_processuridine metabolic process
A0047847molecular_functiondeoxyuridine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE BAU A 400
ChainResidue
AHIS42
AGLU254
AMET255
AASP285
AILE287
AHOH407
AHOH465
AHOH486
AMET116
ATHR147
ASER148
AGLY149
APHE219
AGLN223
AARG225
AILE253

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 1
ChainResidue
AHIS79
AHIS212
AALA248
AHOH354
AHOH399
AHOH471

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CO A 2
ChainResidue
AASP33
AHIS133
AHOH383
AHOH437
AHOH488
AHOH521

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 315
ChainResidue
AASP280
AASP283
AHOH516
AHOH532
AHOH579
AHOH590
AHOH598

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. ShGMGiPSiSImlhEL
ChainResidueDetails
ASER113-LEU128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:21855639, ECO:0007744|PDB:3P0E
ChainResidueDetails
AGLY66
AARG100
AARG144

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:21855639, ECO:0007744|PDB:2XRF, ECO:0007744|PDB:3P0E, ECO:0007744|PDB:3P0F
ChainResidueDetails
ASER148
AGLN223

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PDB entries from 2024-07-24

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