eF-site ID 2akz-AB PDB Code 2akz Chain A, B click to enlarge Title Fluoride Inhibition of Enolase: Crystal Structure of the Inhibitory Complex Classification LYASE Compound Gamma enolase Source Homo sapiens (Human) (ENOG_HUMAN) Sequence A:  SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGAST GIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSG LSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKA GAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIV IGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQ DFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLT VTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQ ENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLMRIEEELGDEARFAGHNFRNPSVLHH B:  SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGAST GIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSG LSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKA GAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIV IGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQ DFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLT VTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQ ENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLMRIEEELGDEARFAGHNFRNPSV Description Functional site 1) chain A residue 244 type sequence D description BINDING SITE FOR RESIDUE MG A 440 source : AC1 2) chain A residue 292 type sequence E description BINDING SITE FOR RESIDUE MG A 440 source : AC1 3) chain A residue 317 type sequence D description BINDING SITE FOR RESIDUE MG A 440 source : AC1 4) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE MG A 440 source : AC1 5) chain A residue 39 type sequence S description BINDING SITE FOR RESIDUE MG A 441 source : AC2 6) chain B residue 1244 type sequence D description BINDING SITE FOR RESIDUE MG B 1440 source : AC3 7) chain B residue 1292 type sequence E description BINDING SITE FOR RESIDUE MG B 1440 source : AC3 8) chain B residue 1317 type sequence D description BINDING SITE FOR RESIDUE MG B 1440 source : AC3 9) chain B residue 1342 type sequence K description BINDING SITE FOR RESIDUE MG B 1440 source : AC3 10) chain B residue 1039 type sequence S description BINDING SITE FOR RESIDUE MG B 1441 source : AC4 11) chain B residue 1317 type sequence D description BINDING SITE FOR RESIDUE MG B 1441 source : AC4 12) chain A residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 13) chain A residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 14) chain A residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 15) chain A residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 16) chain A residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 17) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 18) chain A residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 19) chain A residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 20) chain B residue 1037 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 21) chain B residue 1038 type sequence A description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 22) chain B residue 1039 type sequence S description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 23) chain B residue 1157 type sequence H description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 24) chain B residue 1165 type sequence Q description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 25) chain B residue 1342 type sequence K description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 26) chain B residue 1371 type sequence R description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 27) chain B residue 1372 type sequence S description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 28) chain A residue 39 type sequence S description BINDING SITE FOR RESIDUE F A 444 source : AC7 29) chain A residue 165 type sequence Q description BINDING SITE FOR RESIDUE F A 444 source : AC7 30) chain A residue 244 type sequence D description BINDING SITE FOR RESIDUE F A 444 source : AC7 31) chain A residue 317 type sequence D description BINDING SITE FOR RESIDUE F A 444 source : AC7 32) chain A residue 166 type sequence E description BINDING SITE FOR RESIDUE F A 445 source : AC8 33) chain A residue 244 type sequence D description BINDING SITE FOR RESIDUE F A 445 source : AC8 34) chain A residue 292 type sequence E description BINDING SITE FOR RESIDUE F A 445 source : AC8 35) chain A residue 317 type sequence D description BINDING SITE FOR RESIDUE F A 445 source : AC8 36) chain A residue 340 type sequence L description BINDING SITE FOR RESIDUE F A 445 source : AC8 37) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE F A 445 source : AC8 38) chain A residue 393 type sequence K description BINDING SITE FOR RESIDUE F A 445 source : AC8 39) chain B residue 1039 type sequence S description BINDING SITE FOR RESIDUE F B 1444 source : AC9 40) chain B residue 1165 type sequence Q description BINDING SITE FOR RESIDUE F B 1444 source : AC9 41) chain B residue 1244 type sequence D description BINDING SITE FOR RESIDUE F B 1444 source : AC9 42) chain B residue 1317 type sequence D description BINDING SITE FOR RESIDUE F B 1444 source : AC9 43) chain B residue 1166 type sequence E description BINDING SITE FOR RESIDUE F B 1445 source : BC1 44) chain B residue 1244 type sequence D description BINDING SITE FOR RESIDUE F B 1445 source : BC1 45) chain B residue 1292 type sequence E description BINDING SITE FOR RESIDUE F B 1445 source : BC1 46) chain B residue 1317 type sequence D description BINDING SITE FOR RESIDUE F B 1445 source : BC1 47) chain B residue 1340 type sequence L description BINDING SITE FOR RESIDUE F B 1445 source : BC1 48) chain B residue 1342 type sequence K description BINDING SITE FOR RESIDUE F B 1445 source : BC1 49) chain B residue 1393 type sequence K description BINDING SITE FOR RESIDUE F B 1445 source : BC1 50) chain A residue 40 type sequence T description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 51) chain A residue 42 type sequence I description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 52) chain A residue 248 type sequence S description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 53) chain A residue 249 type sequence E description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 54) chain A residue 297 type sequence Q description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 55) chain A residue 339-352 type prosite sequence LLLKVNQIGSVTEA description ENOLASE Enolase signature. LLLKvNQIGSVTEA source prosite : PS00164 56) chain A residue 210 type ACT_SITE sequence G description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 57) chain B residue 1210 type ACT_SITE sequence G description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 60 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 59) chain A residue 89 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 60) chain A residue 228 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 61) chain B residue 1060 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 62) chain B residue 1089 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 63) chain B residue 1228 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 64) chain A residue 197 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 65) chain A residue 199 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 66) chain B residue 1197 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 67) chain B residue 1199 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 68) chain A residue 202 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI12 69) chain B residue 1202 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI12 70) chain A residue 233 type MOD_RES sequence A description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI13 71) chain B residue 1233 type MOD_RES sequence A description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI13 72) chain A residue 263 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 73) chain B residue 1263 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 74) chain A residue 287 type MOD_RES sequence P description Phosphotyrosine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI15 75) chain B residue 1287 type MOD_RES sequence P description Phosphotyrosine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI15 76) chain A residue 291 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI16 77) chain B residue 1291 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI16 78) chain A residue 335 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 79) chain A residue 343 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 80) chain A residue 406 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 81) chain B residue 1335 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 82) chain B residue 1343 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 83) chain B residue 1406 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 84) chain A residue 202 type CROSSLNK sequence D description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI18 85) chain B residue 1202 type CROSSLNK sequence D description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI18 86) chain A residue 343 type ACT_SITE sequence V description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 87) chain B residue 1343 type ACT_SITE sequence V description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 88) chain A residue 40 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI3 89) chain B residue 1040 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI3 90) chain A residue 158 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 91) chain B residue 1318 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 92) chain B residue 1370 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 93) chain B residue 1394 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 94) chain A residue 167 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 95) chain A residue 293 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 96) chain A residue 318 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 97) chain A residue 370 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 98) chain A residue 394 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 99) chain B residue 1158 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 100) chain B residue 1167 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 101) chain B residue 1293 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 102) chain A residue 245 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI5 103) chain B residue 1245 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI5 104) chain A residue 2 type MOD_RES sequence I description N-acetylserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI6 105) chain B residue 1002 type MOD_RES sequence I description N-acetylserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI6 106) chain A residue 5 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 107) chain A residue 64 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 108) chain A residue 193 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 109) chain A residue 256 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 110) chain B residue 1005 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 111) chain B residue 1064 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 112) chain B residue 1193 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 113) chain B residue 1256 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 114) chain A residue 26 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI8 115) chain B residue 1026 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI8 116) chain A residue 44 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI9 117) chain B residue 1044 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI9

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