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2BSX

Crystal structure of the Plasmodium falciparum purine nucleoside phosphorylase complexed with inosine

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
A0016757molecular_functionglycosyltransferase activity
A0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
A0047975molecular_functionguanosine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NOS A1248
ChainResidue
AHIS7
ATRP212
AARG45
ASER91
ACYS92
AGLY93
ATYR160
AMET183
AGLU184
AASP206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:24416224
ChainResidueDetails
AASP206

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:24416224, ECO:0000305|Ref.7, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC
ChainResidueDetails
AHIS7

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: in other chain => ECO:0000269|PubMed:24416224, ECO:0000269|Ref.7, ECO:0000305|PubMed:14982926, ECO:0000305|PubMed:19575810, ECO:0007744|PDB:1NW4, ECO:0007744|PDB:1Q1G, ECO:0007744|PDB:3ENZ, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC
ChainResidueDetails
AGLY23

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24416224, ECO:0000269|Ref.7, ECO:0000305|PubMed:14982926, ECO:0000305|PubMed:19575810, ECO:0007744|PDB:1NW4, ECO:0007744|PDB:1Q1G, ECO:0007744|PDB:3ENZ, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC
ChainResidueDetails
AARG45

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: in other chain => ECO:0000269|PubMed:24416224, ECO:0000269|PubMed:29440412, ECO:0000269|Ref.7, ECO:0000305|PubMed:14982926, ECO:0000305|PubMed:19575810, ECO:0007744|PDB:1NW4, ECO:0007744|PDB:1Q1G, ECO:0007744|PDB:3ENZ, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC, ECO:0007744|PDB:6AQS, ECO:0007744|PDB:6AQU
ChainResidueDetails
AARG88

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: in other chain => ECO:0000269|PubMed:16131758, ECO:0000305|PubMed:24416224, ECO:0000305|Ref.7, ECO:0007744|PDB:2BSX, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC
ChainResidueDetails
AMET183

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 16131758
ChainResidueDetails
AASP206

site_idMCSA1
Number of Residues4
DetailsM-CSA 695
ChainResidueDetails
AARG27electrostatic stabiliser
AARG45electrostatic stabiliser
AARG88electrostatic stabiliser
AASP206proton acceptor, proton donor

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PDB entries from 2024-07-24

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