eF-site ID 2psn-A PDB Code 2psn Chain A click to enlarge Title Crystal structure of enolase1 Classification LYASE Compound Alpha-enolase Source Homo sapiens (Human) (ENOA_HUMAN) Sequence A:  SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGAST GIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKK LNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKA GAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGN KLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYG KDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVV IGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYK SFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLT VTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQ ANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLLRIEEELGSKAKFAGRNFRNPLA Description Functional site 1) chain A residue 165 type sequence Q description BINDING SITE FOR RESIDUE MG A 701 source : AC1 2) chain A residue 244 type sequence D description BINDING SITE FOR RESIDUE MG A 701 source : AC1 3) chain A residue 292 type sequence E description BINDING SITE FOR RESIDUE MG A 701 source : AC1 4) chain A residue 317 type sequence D description BINDING SITE FOR RESIDUE MG A 701 source : AC1 5) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE MG A 701 source : AC1 6) chain A residue 39 type sequence S description BINDING SITE FOR RESIDUE MG A 702 source : AC2 7) chain A residue 317 type sequence D description BINDING SITE FOR RESIDUE MG A 702 source : AC2 8) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE MG A 702 source : AC2 9) chain A residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 10) chain A residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 11) chain A residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 12) chain A residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 13) chain A residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 14) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 15) chain A residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 16) chain A residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 17) chain A residue 339-352 type prosite sequence LLLKVNQIGSVTES description ENOLASE Enolase signature. LLLKvNQIGSVTES source prosite : PS00164 18) chain A residue 209 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 91 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 20) chain A residue 334 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 21) chain A residue 342 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 22) chain A residue 405 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 23) chain A residue 201 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI11 24) chain A residue 232 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI12 25) chain A residue 253 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 26) chain A residue 262 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI14 27) chain A residue 271 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 28) chain A residue 280 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI16 29) chain A residue 290 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 30) chain A residue 201 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI18 31) chain A residue 342 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 39 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 244 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 157 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 166 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 292 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 317 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 369 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 39) chain A residue 393 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 40) chain A residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000269|Ref.14, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI5 41) chain A residue 4 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 42) chain A residue 63 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 43) chain A residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 44) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 45) chain A residue 192 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 46) chain A residue 198 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 47) chain A residue 255 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 48) chain A residue 284 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 49) chain A residue 26 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 50) chain A residue 43 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 51) chain A residue 286 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 52) chain A residue 59 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 53) chain A residue 88 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 54) chain A residue 227 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 55) chain A residue 419 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9

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