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3ONV

Crystal structure of E. Coli purine nucleoside phosphorylase with SO4

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006152biological_processpurine nucleoside catabolic process
A0006974biological_processDNA damage response
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016020cellular_componentmembrane
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0019686biological_processpurine nucleoside interconversion
A0042278biological_processpurine nucleoside metabolic process
A0042802molecular_functionidentical protein binding
A0047975molecular_functionguanosine phosphorylase activity
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006152biological_processpurine nucleoside catabolic process
B0006974biological_processDNA damage response
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0016020cellular_componentmembrane
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0019686biological_processpurine nucleoside interconversion
B0042278biological_processpurine nucleoside metabolic process
B0042802molecular_functionidentical protein binding
B0047975molecular_functionguanosine phosphorylase activity
C0003824molecular_functioncatalytic activity
C0004731molecular_functionpurine-nucleoside phosphorylase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006139biological_processnucleobase-containing compound metabolic process
C0006152biological_processpurine nucleoside catabolic process
C0006974biological_processDNA damage response
C0009116biological_processnucleoside metabolic process
C0009164biological_processnucleoside catabolic process
C0016020cellular_componentmembrane
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0019686biological_processpurine nucleoside interconversion
C0042278biological_processpurine nucleoside metabolic process
C0042802molecular_functionidentical protein binding
C0047975molecular_functionguanosine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 238
ChainResidue
AGLY20
AARG87
AGLY89
ASER90
AHOH344
AHOH664
AHOH754
CARG43

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 238
ChainResidue
BARG43
BARG87
BGLY89
BSER90
BHOH348
BHOH354
BHOH558
BHOH617
BHOH634
BGLY20

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 239
ChainResidue
BTHR219
BASN222
BHOH311
BHOH537

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 238
ChainResidue
AARG43
CGLY20
CARG87
CGLY89
CSER90
CHOH370
CHOH444
CHOH728

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 239
ChainResidue
CARG217
CGLN218
CGLN218
CHOH279
CHOH559

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL
ChainResidueDetails
AGLY61-LEU76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572
ChainResidueDetails
AASP204
BASP204
CASP204

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
ChainResidueDetails
AHIS4
BHIS4
CHIS4

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
ChainResidueDetails
AGLY20
AARG24
AARG87
BGLY20
BARG24
BARG87
CGLY20
CARG24
CARG87

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
ChainResidueDetails
AARG43
BARG43
CARG43

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
ChainResidueDetails
AGLU179
ASER203
BGLU179
BSER203
CGLU179
CSER203

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572
ChainResidueDetails
AARG217
BARG217
CARG217

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS26
BLYS26
CLYS26

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 375
ChainResidueDetails
AGLY20electrostatic stabiliser
AARG24electrostatic stabiliser
AARG43electrostatic stabiliser
AARG87electrostatic stabiliser
ASER90electrostatic stabiliser
AASP204proton shuttle (general acid/base)
AARG217enhance reactivity

site_idMCSA2
Number of Residues7
DetailsM-CSA 375
ChainResidueDetails
BGLY20electrostatic stabiliser
BARG24electrostatic stabiliser
BARG43electrostatic stabiliser
BARG87electrostatic stabiliser
BSER90electrostatic stabiliser
BASP204proton shuttle (general acid/base)
BARG217enhance reactivity

site_idMCSA3
Number of Residues7
DetailsM-CSA 375
ChainResidueDetails
CGLY20electrostatic stabiliser
CARG24electrostatic stabiliser
CARG43electrostatic stabiliser
CARG87electrostatic stabiliser
CSER90electrostatic stabiliser
CASP204proton shuttle (general acid/base)
CARG217enhance reactivity

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PDB entries from 2024-07-17

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