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6AQU

Crystal Structure of Plasmodium falciparum purine nucleoside phosphorylase: The M183L mutant

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue PO4 A 301
ChainResidue
AGLY23
AARG27
AARG88
AGLY90
ASER91

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 B 301
ChainResidue
BALA89
BGLY90
BSER91
BGLY23
BASP24
BARG27
BARG88

site_idAC3
Number of Residues2
Detailsbinding site for residue PO4 B 302
ChainResidue
BHIS119
BGLY124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"30602534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZNI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"30602534","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5ZNC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5ZNI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"Q8I3X4","evidenceCode":"ECO:0000250"}]}
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

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PDB entries from 2026-01-21

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