eF-site ID 2akz-B PDB Code 2akz Chain B click to enlarge Title Fluoride Inhibition of Enolase: Crystal Structure of the Inhibitory Complex Classification LYASE Compound Gamma enolase Source null (ENOG_HUMAN) Sequence B:  SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGAST GIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSG LSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKA GAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIV IGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQ DFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLT VTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQ ENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLMRIEEELGDEARFAGHNFRNPSV Description Functional site 1) chain B residue 1244 type sequence D description BINDING SITE FOR RESIDUE MG B 1440 source : AC3 2) chain B residue 1292 type sequence E description BINDING SITE FOR RESIDUE MG B 1440 source : AC3 3) chain B residue 1317 type sequence D description BINDING SITE FOR RESIDUE MG B 1440 source : AC3 4) chain B residue 1342 type sequence K description BINDING SITE FOR RESIDUE MG B 1440 source : AC3 5) chain B residue 1039 type sequence S description BINDING SITE FOR RESIDUE MG B 1441 source : AC4 6) chain B residue 1317 type sequence D description BINDING SITE FOR RESIDUE MG B 1441 source : AC4 7) chain B residue 1037 type sequence G description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 8) chain B residue 1038 type sequence A description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 9) chain B residue 1039 type sequence S description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 10) chain B residue 1157 type sequence H description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 11) chain B residue 1165 type sequence Q description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 12) chain B residue 1342 type sequence K description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 13) chain B residue 1371 type sequence R description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 14) chain B residue 1372 type sequence S description BINDING SITE FOR RESIDUE PO4 B 1442 source : AC6 15) chain B residue 1039 type sequence S description BINDING SITE FOR RESIDUE F B 1444 source : AC9 16) chain B residue 1165 type sequence Q description BINDING SITE FOR RESIDUE F B 1444 source : AC9 17) chain B residue 1244 type sequence D description BINDING SITE FOR RESIDUE F B 1444 source : AC9 18) chain B residue 1317 type sequence D description BINDING SITE FOR RESIDUE F B 1444 source : AC9 19) chain B residue 1166 type sequence E description BINDING SITE FOR RESIDUE F B 1445 source : BC1 20) chain B residue 1244 type sequence D description BINDING SITE FOR RESIDUE F B 1445 source : BC1 21) chain B residue 1292 type sequence E description BINDING SITE FOR RESIDUE F B 1445 source : BC1 22) chain B residue 1317 type sequence D description BINDING SITE FOR RESIDUE F B 1445 source : BC1 23) chain B residue 1340 type sequence L description BINDING SITE FOR RESIDUE F B 1445 source : BC1 24) chain B residue 1342 type sequence K description BINDING SITE FOR RESIDUE F B 1445 source : BC1 25) chain B residue 1393 type sequence K description BINDING SITE FOR RESIDUE F B 1445 source : BC1 26) chain B residue 1263 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 27) chain B residue 1287 type MOD_RES sequence P description Phosphotyrosine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI15 28) chain B residue 1291 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI16 29) chain B residue 1335 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 30) chain B residue 1343 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 31) chain B residue 1406 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 32) 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 33) chain B residue 1210 type ACT_SITE sequence G description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 1343 type ACT_SITE sequence V description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 1040 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI3 36) chain B residue 1318 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 1370 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 1394 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 39) chain B residue 1158 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 40) chain B residue 1167 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 41) chain B residue 1293 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 42) chain B residue 1245 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI5 43) chain B residue 1002 type MOD_RES sequence I description N-acetylserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI6 44) chain B residue 1005 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 45) chain B residue 1064 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 46) chain B residue 1193 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 47) chain B residue 1256 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 48) chain B residue 1026 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI8 49) chain B residue 1044 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI9 50) chain B residue 1060 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 51) chain B residue 1089 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 52) chain B residue 1228 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 53) chain B residue 1197 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 54) chain B residue 1199 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 55) chain B residue 1202 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI12 56) chain B residue 1233 type MOD_RES sequence A description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI13

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