eF-site ID 1nw4-B PDB Code 1nw4 Chain B click to enlarge Title Crystal Structure of Plasmodium falciparum Purine Nucleoside Phosphorylase in complex with ImmH and Sulfate Classification TRANSFERASE Compound uridine phosphorylase, putative Source Plasmodium falciparum (isolate 3D7) (Q8I3X4_PLAF7) Sequence B:  NLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLA YNREYKSVECHYKGQKFLCVSHGVGSAGCAVCFEELCQNG AKVIIRAGSCGSLQPDLIKRGDICICNAAVREDRVSHLLI HGDFPAVGDFDVYDTLNKCAQELNVPVFNGISVSSDMYYP NKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGI LIVDGCPFKWDEGDFDNNLVPHQLENMIKIALGACAKLAT KYA Description Functional site 1) chain B residue 45 type sequence R description BINDING SITE FOR RESIDUE SO4 A 401 source : AC1 2) chain B residue 23 type sequence G description BINDING SITE FOR RESIDUE SO4 B 402 source : AC2 3) chain B residue 88 type sequence R description BINDING SITE FOR RESIDUE SO4 B 402 source : AC2 4) chain B residue 90 type sequence G description BINDING SITE FOR RESIDUE SO4 B 402 source : AC2 5) chain B residue 91 type sequence S description BINDING SITE FOR RESIDUE SO4 B 402 source : AC2 6) chain B residue 124 type sequence G description BINDING SITE FOR RESIDUE SO4 B 407 source : AC7 7) chain B residue 125 type sequence D description BINDING SITE FOR RESIDUE SO4 B 407 source : AC7 8) chain B residue 101 type sequence K description BINDING SITE FOR RESIDUE SO4 B 410 source : BC1 9) chain B residue 102 type sequence R description BINDING SITE FOR RESIDUE SO4 B 410 source : BC1 10) chain B residue 216 type sequence D description BINDING SITE FOR RESIDUE SO4 B 410 source : BC1 11) chain B residue 169 type sequence R description BINDING SITE FOR RESIDUE SO4 C 418 source : BC9 12) chain B residue 7 type sequence H description BINDING SITE FOR RESIDUE IMH A 301 source : CC2 13) chain B residue 88 type sequence R description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 14) chain B residue 91 type sequence S description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 15) chain B residue 92 type sequence C description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 16) chain B residue 93 type sequence G description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 17) chain B residue 160 type sequence Y description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 18) chain B residue 182 type sequence E description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 19) chain B residue 183 type sequence M description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 20) chain B residue 184 type sequence E description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 21) chain B residue 206 type sequence D description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 22) chain B residue 212 type sequence W description BINDING SITE FOR RESIDUE IMH B 302 source : CC3 23) chain B residue 44 type sequence N description BINDING SITE FOR RESIDUE IPA B 501 source : CC8 24) chain B residue 45 type sequence R description BINDING SITE FOR RESIDUE IPA B 501 source : CC8 25) chain B residue 116 type sequence R description BINDING SITE FOR RESIDUE IPA B 507 source : DC5 26) chain B residue 119 type sequence H description BINDING SITE FOR RESIDUE IPA B 507 source : DC5 27) chain B residue 119 type sequence H description BINDING SITE FOR RESIDUE IPA B 508 source : DC6 28) chain B residue 123 type sequence H description BINDING SITE FOR RESIDUE IPA B 508 source : DC6 29) chain B residue 169 type sequence R description BINDING SITE FOR RESIDUE IPA A 509 source : DC7 30) chain B residue 169 type sequence R description BINDING SITE FOR RESIDUE IPA B 515 source : EC4 31) chain B residue 27 type catalytic sequence R description 695 source MCSA : MCSA2 32) chain B residue 45 type catalytic sequence R description 695 source MCSA : MCSA2 33) chain B residue 88 type catalytic sequence R description 695 source MCSA : MCSA2 34) chain B residue 206 type catalytic sequence D description 695 source MCSA : MCSA2 35) chain B 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 36) chain B 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 37) chain B 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 38) chain B 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 39) chain B 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 40) chain B residue 206 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:24416224 source Swiss-Prot : SWS_FT_FI1

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