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1LV8

Crystal structure of calf spleen purine nucleoside phosphorylase in a new space group with full trimer in the asymmetric unit

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0006166biological_processpurine ribonucleoside salvage
A0009116biological_processnucleoside metabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0047975molecular_functionguanosine phosphorylase activity
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0005737cellular_componentcytoplasm
B0006139biological_processnucleobase-containing compound metabolic process
B0006166biological_processpurine ribonucleoside salvage
B0009116biological_processnucleoside metabolic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0047975molecular_functionguanosine phosphorylase activity
C0003824molecular_functioncatalytic activity
C0004731molecular_functionpurine-nucleoside phosphorylase activity
C0005737cellular_componentcytoplasm
C0006139biological_processnucleobase-containing compound metabolic process
C0006166biological_processpurine ribonucleoside salvage
C0009116biological_processnucleoside metabolic process
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0047975molecular_functionguanosine phosphorylase activity
D0003824molecular_functioncatalytic activity
D0004731molecular_functionpurine-nucleoside phosphorylase activity
D0005737cellular_componentcytoplasm
D0006139biological_processnucleobase-containing compound metabolic process
D0006166biological_processpurine ribonucleoside salvage
D0009116biological_processnucleoside metabolic process
D0016757molecular_functionglycosyltransferase activity
D0016763molecular_functionpentosyltransferase activity
D0047975molecular_functionguanosine phosphorylase activity
E0003824molecular_functioncatalytic activity
E0004731molecular_functionpurine-nucleoside phosphorylase activity
E0005737cellular_componentcytoplasm
E0006139biological_processnucleobase-containing compound metabolic process
E0006166biological_processpurine ribonucleoside salvage
E0009116biological_processnucleoside metabolic process
E0016757molecular_functionglycosyltransferase activity
E0016763molecular_functionpentosyltransferase activity
E0047975molecular_functionguanosine phosphorylase activity
F0003824molecular_functioncatalytic activity
F0004731molecular_functionpurine-nucleoside phosphorylase activity
F0005737cellular_componentcytoplasm
F0006139biological_processnucleobase-containing compound metabolic process
F0006166biological_processpurine ribonucleoside salvage
F0009116biological_processnucleoside metabolic process
F0016757molecular_functionglycosyltransferase activity
F0016763molecular_functionpentosyltransferase activity
F0047975molecular_functionguanosine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 7001
ChainResidue
AGLU58
DSER51
DGLU58
DHOH7032
DHOH7034
DHOH7100

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 7002
ChainResidue
AHOH7069
DGLU58
DHOH7085
ASER51
AGLU58
AHOH7052

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 7003
ChainResidue
CGLU2058
EHOH155
EHOH439
EHOH693
ESER1051
EGLU1058

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 7004
ChainResidue
CHOH262
CHOH305
CHOH718
CSER2051
CGLU2058
EGLU1058

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 7005
ChainResidue
BHOH363
BSER1051
BGLU1058
FHOH376
FHOH588
FGLU2058

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA F 7006
ChainResidue
BGLU1058
FHOH207
FHOH287
FHOH368
FSER2051
FGLU2058

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 9PP A 3001
ChainResidue
AGLY32
ASER33
AHIS86
AASN115
AALA116
AALA117
AGLY118
ALEU195
APHE200
AGLU201
AGLY218
AMET219
ASER220
AASN243
AHOH7033
AHOH7050
AHOH7122

site_idAC8
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 9PP B 3002
ChainResidue
BHOH105
BHOH173
BHOH319
BHOH322
BGLY1032
BSER1033
BHIS1086
BASN1115
BALA1116
BALA1117
BGLY1118
BLEU1195
BPHE1200
BGLU1201
BVAL1217
BGLY1218
BMET1219
BSER1220
BASN1243

site_idAC9
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 9PP C 3003
ChainResidue
CHOH96
CHOH103
CHOH460
CHOH464
CGLY2032
CSER2033
CHIS2086
CASN2115
CALA2116
CALA2117
CGLY2118
CLEU2195
CPHE2200
CGLU2201
CVAL2217
CGLY2218
CMET2219
CSER2220
CASN2243

site_idBC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 9PP E 3004
ChainResidue
EALA1116
ELEU1195
EPHE1200
EGLU1201
EVAL1217
EGLY1218
EMET1219
ESER1220
EASN1243
EHOH222
EHOH236
EHOH620
EHOH674
EGLY1032
ESER1033
EHIS1086
EASN1115

site_idBC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 9PP F 3005
ChainResidue
FHOH138
FHOH150
FHOH338
FHOH691
FGLY2032
FSER2033
FHIS2086
FASN2115
FALA2116
FALA2117
FGLY2118
FLEU2195
FPHE2200
FGLU2201
FVAL2217
FGLY2218
FMET2219
FSER2220
FASN2243

site_idBC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 9PP D 3006
ChainResidue
DGLY32
DSER33
DHIS86
DASN115
DALA116
DALA117
DGLY118
DLEU195
DPHE200
DGLU201
DMET219
DSER220
DASN243
DHOH7044
DHOH7055
DHOH7058
DHOH7068

Functional Information from PROSITE/UniProt
site_idPS01240
Number of Residues42
DetailsPNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypFwkvTfpVrVfrllGvet.LVvtNAaGGL
ChainResidueDetails
AVAL79-LEU120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP
ChainResidueDetails
ASER33
BSER1033
CSER2033
DSER33
ESER1033
FSER2033

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP
ChainResidueDetails
AHIS64
BHIS1064
CHIS2064
DHIS64
EHIS1064
FHIS2064

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP
ChainResidueDetails
AARG84
DARG84
DALA116
DSER220
EARG1084
EALA1116
ESER1220
FARG2084
FALA2116
FSER2220
AALA116
ASER220
BARG1084
BALA1116
BSER1220
CARG2084
CALA2116
CSER2220

site_idSWS_FT_FI4
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T
ChainResidueDetails
ATYR88
DTYR88
DMET219
DHIS257
ETYR1088
EMET1219
EHIS1257
FTYR2088
FMET2219
FHIS2257
AMET219
AHIS257
BTYR1088
BMET1219
BHIS1257
CTYR2088
CMET2219
CHIS2257

site_idSWS_FT_FI5
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0000305|PubMed:9020983, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, ECO:0007744|PDB:1VFN
ChainResidueDetails
AGLU201
EASN1243
FGLU2201
FASN2243
AASN243
BGLU1201
BASN1243
CGLU2201
CASN2243
DGLU201
DASN243
EGLU1201

site_idSWS_FT_FI6
Number of Residues6
DetailsSITE: Important for substrate specificity => ECO:0000250|UniProtKB:P00491
ChainResidueDetails
AASN243
BASN1243
CASN2243
DASN243
EASN1243
FASN2243

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P00491
ChainResidueDetails
AMET1
BMET1001
CMET2001
DMET1
EMET1001
FMET2001

site_idSWS_FT_FI8
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00491
ChainResidueDetails
ASER251
BSER1251
CSER2251
DSER251
ESER1251
FSER2251

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
AASN243
AHIS86
AGLU89

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
DASN243
DASP248

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
EASP1248
EASN1243

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
FASN2243
FASP2248

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
BASN1243
BGLU1089
BHIS1086

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
CHIS2086
CASN2243
CGLU2089

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
DASN243
DHIS86
DGLU89

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
EASN1243
EGLU1089
EHIS1086

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
FHIS2086
FASN2243
FGLU2089

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
AASN243
AASP248

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
BASP1248
BASN1243

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
CASN2243
CASP2248

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PDB entries from 2024-10-30

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