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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3ENZ

Arsenolytic structure of Plasmodium falciparum purine nucleoside phosphorylase with hypoxanthine, ribose and arsenate ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0004850molecular_functionuridine phosphorylase activity
A0005829cellular_componentcytosol
A0006148biological_processinosine catabolic process
A0006166biological_processpurine ribonucleoside salvage
A0006195biological_processpurine nucleotide catabolic process
A0006218biological_processuridine catabolic process
A0009116biological_processnucleoside metabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
A0047975molecular_functionguanosine phosphorylase activity
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0004850molecular_functionuridine phosphorylase activity
B0005829cellular_componentcytosol
B0006148biological_processinosine catabolic process
B0006166biological_processpurine ribonucleoside salvage
B0006195biological_processpurine nucleotide catabolic process
B0006218biological_processuridine catabolic process
B0009116biological_processnucleoside metabolic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
B0047975molecular_functionguanosine phosphorylase activity
C0003824molecular_functioncatalytic activity
C0004731molecular_functionpurine-nucleoside phosphorylase activity
C0004850molecular_functionuridine phosphorylase activity
C0005829cellular_componentcytosol
C0006148biological_processinosine catabolic process
C0006166biological_processpurine ribonucleoside salvage
C0006195biological_processpurine nucleotide catabolic process
C0006218biological_processuridine catabolic process
C0009116biological_processnucleoside metabolic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
C0047975molecular_functionguanosine phosphorylase activity
D0003824molecular_functioncatalytic activity
D0004731molecular_functionpurine-nucleoside phosphorylase activity
D0004850molecular_functionuridine phosphorylase activity
D0005829cellular_componentcytosol
D0006148biological_processinosine catabolic process
D0006166biological_processpurine ribonucleoside salvage
D0006195biological_processpurine nucleotide catabolic process
D0006218biological_processuridine catabolic process
D0009116biological_processnucleoside metabolic process
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
D0047975molecular_functionguanosine phosphorylase activity
E0003824molecular_functioncatalytic activity
E0004731molecular_functionpurine-nucleoside phosphorylase activity
E0004850molecular_functionuridine phosphorylase activity
E0005829cellular_componentcytosol
E0006148biological_processinosine catabolic process
E0006166biological_processpurine ribonucleoside salvage
E0006195biological_processpurine nucleotide catabolic process
E0006218biological_processuridine catabolic process
E0009116biological_processnucleoside metabolic process
E0016740molecular_functiontransferase activity
E0016757molecular_functionglycosyltransferase activity
E0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
E0047975molecular_functionguanosine phosphorylase activity
F0003824molecular_functioncatalytic activity
F0004731molecular_functionpurine-nucleoside phosphorylase activity
F0004850molecular_functionuridine phosphorylase activity
F0005829cellular_componentcytosol
F0006148biological_processinosine catabolic process
F0006166biological_processpurine ribonucleoside salvage
F0006195biological_processpurine nucleotide catabolic process
F0006218biological_processuridine catabolic process
F0009116biological_processnucleoside metabolic process
F0016740molecular_functiontransferase activity
F0016757molecular_functionglycosyltransferase activity
F0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
F0047975molecular_functionguanosine phosphorylase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PubMed","id":"14982926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19575810","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NW4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ENZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PubMed","id":"14982926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19575810","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NW4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ENZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues18
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29440412","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PubMed","id":"14982926","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19575810","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NW4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ENZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6AQS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6AQU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"16131758","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24416224","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"NOV-2010","submissionDatabase":"PDB data bank","title":"Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase in complex with DADMe-ImmG.","authors":["Ho M.","Edwards A.A.","Almo S.C.","Schramm V.L."]}},{"source":"PDB","id":"2BSX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PHC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 695
ChainResidueDetails
AARG27electrostatic stabiliser
AARG45electrostatic stabiliser
AARG88electrostatic stabiliser
AASP206proton acceptor, proton donor
site_idMCSA2
Number of Residues4
DetailsM-CSA 695
ChainResidueDetails
BARG27electrostatic stabiliser
BARG45electrostatic stabiliser
BARG88electrostatic stabiliser
BASP206proton acceptor, proton donor
site_idMCSA3
Number of Residues4
DetailsM-CSA 695
ChainResidueDetails
CARG27electrostatic stabiliser
CARG45electrostatic stabiliser
CARG88electrostatic stabiliser
CASP206proton acceptor, proton donor
site_idMCSA4
Number of Residues4
DetailsM-CSA 695
ChainResidueDetails
DARG27electrostatic stabiliser
DARG45electrostatic stabiliser
DARG88electrostatic stabiliser
DASP206proton acceptor, proton donor
site_idMCSA5
Number of Residues4
DetailsM-CSA 695
ChainResidueDetails
EARG27electrostatic stabiliser
EARG45electrostatic stabiliser
EARG88electrostatic stabiliser
EASP206proton acceptor, proton donor
site_idMCSA6
Number of Residues4
DetailsM-CSA 695
ChainResidueDetails
FARG27electrostatic stabiliser
FARG45electrostatic stabiliser
FARG88electrostatic stabiliser
FASP206proton acceptor, proton donor

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