eF-site ID 2akz-A PDB Code 2akz Chain A click to enlarge Title Fluoride Inhibition of Enolase: Crystal Structure of the Inhibitory Complex Classification LYASE Compound Gamma enolase Source null (ENOG_HUMAN) Sequence A:  SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGAST GIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSG LSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKA GAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGN KLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIV IGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQ DFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLT VTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQ ENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLMRIEEELGDEARFAGHNFRNPSVLHH 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 A residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 7) chain A residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 8) chain A residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 9) chain A residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 10) chain A residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 11) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 12) chain A residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 13) chain A residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 A 442 source : AC5 14) chain A residue 39 type sequence S description BINDING SITE FOR RESIDUE F A 444 source : AC7 15) chain A residue 165 type sequence Q description BINDING SITE FOR RESIDUE F A 444 source : AC7 16) chain A residue 244 type sequence D description BINDING SITE FOR RESIDUE F A 444 source : AC7 17) chain A residue 317 type sequence D description BINDING SITE FOR RESIDUE F A 444 source : AC7 18) chain A residue 166 type sequence E description BINDING SITE FOR RESIDUE F A 445 source : AC8 19) chain A residue 244 type sequence D description BINDING SITE FOR RESIDUE F A 445 source : AC8 20) chain A residue 292 type sequence E description BINDING SITE FOR RESIDUE F A 445 source : AC8 21) chain A residue 317 type sequence D description BINDING SITE FOR RESIDUE F A 445 source : AC8 22) chain A residue 340 type sequence L description BINDING SITE FOR RESIDUE F A 445 source : AC8 23) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE F A 445 source : AC8 24) chain A residue 393 type sequence K description BINDING SITE FOR RESIDUE F A 445 source : AC8 25) chain A residue 40 type sequence T description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 26) chain A residue 42 type sequence I description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 27) chain A residue 248 type sequence S description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 28) chain A residue 249 type sequence E description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 29) chain A residue 297 type sequence Q description BINDING SITE FOR RESIDUE TRS A 460 source : BC2 30) chain A residue 263 type MOD_RES sequence P description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 31) chain A residue 287 type MOD_RES sequence P description Phosphotyrosine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI15 32) chain A residue 291 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI16 33) chain A residue 335 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 34) chain A residue 343 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 35) chain A residue 406 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI17 36) 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 37) chain A residue 210 type ACT_SITE sequence G description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 343 type ACT_SITE sequence V description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 40 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 158 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 167 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 42) chain A residue 293 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 43) chain A residue 318 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 370 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 394 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 245 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI5 47) chain A residue 2 type MOD_RES sequence I description N-acetylserine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI6 48) chain A residue 5 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 49) chain A residue 64 type MOD_RES sequence A description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 50) chain A residue 193 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 51) chain A residue 256 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI7 52) chain A residue 26 type MOD_RES sequence A description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI8 53) chain A residue 44 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI9 54) chain A residue 60 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 55) chain A residue 89 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 56) chain A residue 228 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 57) chain A residue 197 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 58) chain A residue 199 type MOD_RES sequence Y description N6-acetyllysine => ECO:0000250|UniProtKB:P17183 source Swiss-Prot : SWS_FT_FI11 59) chain A residue 202 type MOD_RES sequence D description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI12 60) chain A residue 233 type MOD_RES sequence A description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733 source Swiss-Prot : SWS_FT_FI13 61) chain A residue 339-352 type prosite sequence LLLKVNQIGSVTEA description ENOLASE Enolase signature. LLLKvNQIGSVTEA source prosite : PS00164

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