eF-site ID 2bsx-A PDB Code 2bsx Chain A click to enlarge Title Crystal structure of the Plasmodium falciparum purine nucleoside phosphorylase complexed with inosine Classification TRANSFERASE Compound PURINE NUCLEOSIDE PHOSPHORYLASE Source (2BSX) Sequence A:  MDNLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVD LAYNREYKSVECHYKGQKFLCVSHGVGSAGCAVCFEELCQ NGAKVIIRAGSCGSLQPDLIKRGDICICNAAVREDRVSHL LIHGDFPAVGDFDVYDTLNKCAQELNVPVFNGISVSSDMY YPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTG GILIVDGCPFKWDELVPHQLENMIKIALGACAKLATKYAL E Description Functional site 1) chain A residue 7 type sequence H description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 2) chain A residue 45 type sequence R description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 3) chain A residue 91 type sequence S description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 4) chain A residue 92 type sequence C description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 5) chain A residue 93 type sequence G description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 6) chain A residue 160 type sequence Y description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 7) chain A residue 183 type sequence M description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 8) chain A residue 184 type sequence E description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 9) chain A residue 206 type sequence D description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 10) chain A residue 212 type sequence W description BINDING SITE FOR RESIDUE NOS A1248 source : AC1 11) chain A residue 27 type catalytic sequence R description 695 source MCSA : MCSA1 12) chain A residue 45 type catalytic sequence R description 695 source MCSA : MCSA1 13) chain A residue 88 type catalytic sequence R description 695 source MCSA : MCSA1 14) chain A residue 206 type catalytic sequence D description 695 source MCSA : MCSA1 15) chain A residue 7 type BINDING sequence H description BINDING => ECO:0000305|PubMed:24416224, ECO:0000305|Ref.7, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC source Swiss-Prot : SWS_FT_FI2 16) chain A residue 206 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:24416224 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 23 type BINDING sequence G description 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 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 45 type BINDING sequence R description 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 source Swiss-Prot : SWS_FT_FI4 19) chain A residue 88 type BINDING sequence R description 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 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 183 type BINDING sequence M description 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 source Swiss-Prot : SWS_FT_FI6

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