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4LZW

X-ray structure uridine phosphorylase from Vibrio cholerae in complex with thymidine at 1.29 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004850molecular_functionuridine phosphorylase activity
A0005737cellular_componentcytoplasm
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
B0003824molecular_functioncatalytic activity
B0004850molecular_functionuridine phosphorylase activity
B0005737cellular_componentcytoplasm
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
C0003824molecular_functioncatalytic activity
C0004850molecular_functionuridine phosphorylase activity
C0005737cellular_componentcytoplasm
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
D0003824molecular_functioncatalytic activity
D0004850molecular_functionuridine phosphorylase activity
D0005737cellular_componentcytoplasm
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
E0003824molecular_functioncatalytic activity
E0004850molecular_functionuridine phosphorylase activity
E0005737cellular_componentcytoplasm
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
F0003824molecular_functioncatalytic activity
F0004850molecular_functionuridine phosphorylase activity
F0005737cellular_componentcytoplasm
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
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE THM A 301
ChainResidue
ATHR93
AILE219
AHOH476
AHOH681
BHIS7
BARG47
AGLY95
APHE161
AGLN165
AARG167
APHE194
AGLU195
AMET196
AGLU197

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EOH A 302
ChainResidue
AARG178
AHOH601
AHOH676
BLEU120
BHOH425
BHOH715
FHOH616

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EOH A 303
ChainResidue
AMET125
AGLU126
AHOH505
FMET125

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
AGLY25
AASP26
AARG29
AHOH493

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 305
ChainResidue
AGLU48
AILE68
ASER72
BGLU48
BILE68
BSER72

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 306
ChainResidue
AASN221

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 307
ChainResidue
AGLN180
AHOH513
AHOH562
AHOH621
AHOH688
CHOH656

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE THM B 301
ChainResidue
AHIS7
AARG47
AHOH516
BTHR93
BGLY95
BPHE161
BGLN165
BARG167
BPHE194
BGLU195
BMET196
BILE220
BHOH426
BHOH442

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EOH B 302
ChainResidue
BMET125
CGLU126

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EOH B 303
ChainResidue
ALEU120
AHOH417
AHOH421
BARG178
BHOH539
BHOH716

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 304
ChainResidue
BGLY25
BASP26
BARG29
BHOH459

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 305
ChainResidue
BGLN180
BHOH454
BHOH503
BHOH524
BHOH559

site_idBC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE THM C 301
ChainResidue
CTHR93
CGLY95
CPHE161
CGLN165
CARG167
CPHE194
CGLU195
CMET196
CGLU197
CILE220
CHOH410
CHOH494
CHOH591
DHIS7
DARG47

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO C 302
ChainResidue
BHOH677
CARG178
CHOH429
CHOH433
CHOH757
CHOH758
DLEU120

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 303
ChainResidue
CGLY25
CASP26
CARG29
CHOH480

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA C 304
ChainResidue
CGLU48
CILE68
CSER72
DGLU48
DILE68
DSER72

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 305
ChainResidue
CMG306
CHOH486
CHOH492
CHOH561
CHOH660

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 306
ChainResidue
CASN102
CMG305
CHOH486
CHOH488
CHOH492

site_idCC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE THM D 301
ChainResidue
CHIS7
CARG47
DILE68
DTHR93
DGLY95
DPHE161
DGLN165
DARG167
DPHE194
DGLU195
DMET196
DGLU197
DILE220
DHOH407
DHOH445
DHOH456
DHOH569

site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EOH D 302
ChainResidue
CLEU120
CHOH437
CHOH761
DARG178
DHOH697

site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL D 303
ChainResidue
CHOH590
DGLY25
DASP26
DARG29
DHOH466

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 304
ChainResidue
DMG305
DHOH470
DHOH528
DHOH568

site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 305
ChainResidue
DASN102
DMG304
DHOH470
DHOH528
DHOH666

site_idCC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE THM E 301
ChainResidue
ETHR93
EGLY95
EPHE161
EGLN165
EARG167
EPHE194
EGLU195
EMET196
EGLU197
EHOH432
EHOH448
FHIS7
FARG47

site_idCC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO E 302
ChainResidue
EMET183
EGLN187
EHOH430
EHOH599
EHOH635

site_idCC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EOH E 303
ChainResidue
EARG178
EHOH676
EHOH684
EHOH706
FLEU120
FHOH416
FHOH422

site_idCC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL E 304
ChainResidue
EGLY25
EASP26
EARG29
EHOH493
FHOH488

site_idDC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG E 305
ChainResidue
EGLN180
EHOH468
EHOH562
EHOH574
EHOH619
EHOH622

site_idDC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE THM F 301
ChainResidue
EHIS7
EARG47
FTHR93
FGLY95
FPHE161
FGLN165
FARG167
FPHE194
FGLU195
FMET196
FGLU197
FILE219
FILE220
FHOH480
FHOH611

site_idDC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EOH F 302
ChainResidue
AHOH600
ELEU120
EHOH421
EHOH423
FARG178
FHOH598
FHOH685

site_idDC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL F 303
ChainResidue
FGLY25
FASP26
FARG29
FHOH585
FHOH686

site_idDC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA F 304
ChainResidue
EGLU48
EILE68
ESER72
FGLU48
FILE68
FSER72

site_idDC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL F 305
ChainResidue
FASN221
FLYS225
FHOH569

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

223532

PDB entries from 2024-08-07

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