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4IP0

X-Ray Structure of the Complex Uridine Phosphorylase from Vibrio cholerae with Phosphate Ion at 1.29 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
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0044206biological_processUMP salvage
A0046872molecular_functionmetal ion binding
A0047847molecular_functiondeoxyuridine phosphorylase activity
B0003824molecular_functioncatalytic activity
B0004850molecular_functionuridine phosphorylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0009166biological_processnucleotide catabolic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0044206biological_processUMP salvage
B0046872molecular_functionmetal ion binding
B0047847molecular_functiondeoxyuridine phosphorylase activity
C0003824molecular_functioncatalytic activity
C0004850molecular_functionuridine phosphorylase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0009116biological_processnucleoside metabolic process
C0009164biological_processnucleoside catabolic process
C0009166biological_processnucleotide catabolic process
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0044206biological_processUMP salvage
C0046872molecular_functionmetal ion binding
C0047847molecular_functiondeoxyuridine phosphorylase activity
D0003824molecular_functioncatalytic activity
D0004850molecular_functionuridine phosphorylase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0009116biological_processnucleoside metabolic process
D0009164biological_processnucleoside catabolic process
D0009166biological_processnucleotide catabolic process
D0016757molecular_functionglycosyltransferase activity
D0016763molecular_functionpentosyltransferase activity
D0044206biological_processUMP salvage
D0046872molecular_functionmetal ion binding
D0047847molecular_functiondeoxyuridine phosphorylase activity
E0003824molecular_functioncatalytic activity
E0004850molecular_functionuridine phosphorylase activity
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0009116biological_processnucleoside metabolic process
E0009164biological_processnucleoside catabolic process
E0009166biological_processnucleotide catabolic process
E0016757molecular_functionglycosyltransferase activity
E0016763molecular_functionpentosyltransferase activity
E0044206biological_processUMP salvage
E0046872molecular_functionmetal ion binding
E0047847molecular_functiondeoxyuridine phosphorylase activity
F0003824molecular_functioncatalytic activity
F0004850molecular_functionuridine phosphorylase activity
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0009116biological_processnucleoside metabolic process
F0009164biological_processnucleoside catabolic process
F0009166biological_processnucleotide catabolic process
F0016757molecular_functionglycosyltransferase activity
F0016763molecular_functionpentosyltransferase activity
F0044206biological_processUMP salvage
F0046872molecular_functionmetal ion binding
F0047847molecular_functiondeoxyuridine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
AGLU48
AILE68
ASER72
BGLU48
BILE68
BSER72

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
CGLN31
AHOH578
AHOH670
AHOH747

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 B 301
ChainResidue
BARG86
BHOH516

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 302
ChainResidue
AARG47
BGLY25
BARG29
BARG90
BVAL91
BGLY92
BTHR93
BHOH439
BHOH489

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
BLYS140
BGLN144
BHOH604
BHOH626
BHOH655

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 304
ChainResidue
BARG177
BHOH457
BHOH505
DARG177
FARG177

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 305
ChainResidue
AGLY92
ATHR93
AHOH550
AHOH564
BARG47
BHOH634

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EOH B 306
ChainResidue
BHOH413
BHOH437
BHOH438

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 C 301
ChainResidue
CGLY25
CARG29
CARG90
CVAL91
CGLY92
CTHR93
CHOH442
CHOH573
CHOH581
DARG47

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 302
ChainResidue
CGLY95
CARG167
CILE220
CEDO303

site_idBC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE EDO C 303
ChainResidue
CTHR94
CGLY95
CPHE161
CGLN165
CPHE194
CGLU195
CMET196
CCL302
CHOH524
CHOH573
CHOH579
CHOH580

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO C 304
ChainResidue
CARG239
CLYS242
CHOH703

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K D 301
ChainResidue
CGLU48
CILE68
CSER72
DGLU48
DILE68
DSER72

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 302
ChainResidue
CHOH458
CHOH517
DHIS46
DHOH443
DHOH533
DHOH586
DHOH676

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA E 301
ChainResidue
EGLU48
EILE68
ESER72
FGLU48
FILE68
FSER72

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 E 302
ChainResidue
EARG90
EGLY92
ETHR93
EHOH441
EHOH581
EHOH627
EHOH731
FARG47

site_idBC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 E 303
ChainResidue
EARG86
EHOH663
EHOH687

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO E 304
ChainResidue
EGLU166
EMET183
EARG222
EHOH693
EHOH706

site_idCC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 F 301
ChainResidue
EARG47
FGLY25
FARG29
FARG90
FVAL91
FGLY92
FTHR93
FHOH467
FHOH575
FHOH585

site_idCC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 F 302
ChainResidue
FLYS140
FGLN144
FHOH520
FHOH523
FHOH527
FHOH588
FHOH643
FHOH658

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL F 303
ChainResidue
FGLY95
FARG167
FILE220
FEDO304

site_idCC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE EDO F 304
ChainResidue
FTHR94
FGLY95
FGLN165
FPHE194
FGLU195
FMET196
FCL303
FHOH575
FHOH577
FHOH578
FHOH579
FHOH585

site_idCC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO F 305
ChainResidue
ASER207
ASER208
AGLY209
BARG174
FASP188
FMET189
FGLY190
FHOH425
FHOH716

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. StGIGgPStSIaveEL
ChainResidueDetails
ASER65-LEU80

225946

PDB entries from 2024-10-09

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