eF-site ID 1nw4-E PDB Code 1nw4 Chain E 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 E:  NLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLA YNREYKSVECHYKGQKFLCVSHGVGSAGCAVCFEELCQNG AKVIIRAGSCGSLQPDLIKRGDICICNAAVREDRVSHLLI HGDFPAVGDFDVYDTLNKCAQELNVPVFNGISVSSDMYYP NKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGI LIVDGCPFKWDEGDFDNNLVPHQLENMIKIALGACAKLAT KYA Description Functional site 1) chain E residue 23 type sequence G description BINDING SITE FOR RESIDUE SO4 E 405 source : AC5 2) chain E residue 88 type sequence R description BINDING SITE FOR RESIDUE SO4 E 405 source : AC5 3) chain E residue 90 type sequence G description BINDING SITE FOR RESIDUE SO4 E 405 source : AC5 4) chain E residue 91 type sequence S description BINDING SITE FOR RESIDUE SO4 E 405 source : AC5 5) chain E residue 45 type sequence R description BINDING SITE FOR RESIDUE SO4 F 406 source : AC6 6) chain E residue 169 type sequence R description BINDING SITE FOR RESIDUE SO4 D 408 source : AC8 7) chain E residue 123 type sequence H description BINDING SITE FOR RESIDUE SO4 E 416 source : BC7 8) chain E residue 124 type sequence G description BINDING SITE FOR RESIDUE SO4 E 416 source : BC7 9) chain E residue 125 type sequence D description BINDING SITE FOR RESIDUE SO4 E 416 source : BC7 10) chain E residue 101 type sequence K description BINDING SITE FOR RESIDUE SO4 E 419 source : CC1 11) chain E residue 102 type sequence R description BINDING SITE FOR RESIDUE SO4 E 419 source : CC1 12) chain E residue 216 type sequence D description BINDING SITE FOR RESIDUE SO4 E 419 source : CC1 13) chain E residue 88 type sequence R description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 14) chain E residue 91 type sequence S description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 15) chain E residue 92 type sequence C description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 16) chain E residue 93 type sequence G description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 17) chain E residue 160 type sequence Y description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 18) chain E residue 182 type sequence E description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 19) chain E residue 183 type sequence M description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 20) chain E residue 184 type sequence E description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 21) chain E residue 206 type sequence D description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 22) chain E residue 212 type sequence W description BINDING SITE FOR RESIDUE IMH E 305 source : CC6 23) chain E residue 7 type sequence H description BINDING SITE FOR RESIDUE IMH F 306 source : CC7 24) chain E residue 44 type sequence N description BINDING SITE FOR RESIDUE IPA E 506 source : DC4 25) chain E residue 45 type sequence R description BINDING SITE FOR RESIDUE IPA E 506 source : DC4 26) chain E residue 169 type sequence R description BINDING SITE FOR RESIDUE IPA F 511 source : DC9 27) chain E residue 119 type sequence H description BINDING SITE FOR RESIDUE IPA E 513 source : EC2 28) chain E residue 123 type sequence H description BINDING SITE FOR RESIDUE IPA E 513 source : EC2 29) chain E residue 169 type sequence R description BINDING SITE FOR RESIDUE IPA D 514 source : EC3 30) chain E residue 25 type catalytic sequence P description 695 source MCSA : MCSA5 31) chain E residue 43 type catalytic sequence Y description 695 source MCSA : MCSA5 32) chain E residue 86 type catalytic sequence I description 695 source MCSA : MCSA5 33) chain E residue 204 type catalytic sequence I description 695 source MCSA : MCSA5 34) chain E residue 43 type BINDING sequence Y 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 35) chain E residue 86 type BINDING sequence I 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 36) chain E residue 181 type BINDING sequence V 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 37) chain E residue 5 type BINDING sequence L description BINDING => ECO:0000305|PubMed:24416224, ECO:0000305|Ref.7, ECO:0007744|PDB:3FOW, ECO:0007744|PDB:3PHC source Swiss-Prot : SWS_FT_FI2 38) chain E residue 21 type BINDING sequence V 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 39) chain E residue 204 type ACT_SITE sequence I description Proton donor => ECO:0000305|PubMed:24416224 source Swiss-Prot : SWS_FT_FI1

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