eF-site ID 2psn-D PDB Code 2psn Chain D click to enlarge Title Crystal structure of enolase1 Classification LYASE Compound Alpha-enolase Source Homo sapiens (Human) (ENOA_HUMAN) Sequence D:  SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGAST GIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKK LNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKA GAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGN KLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYG KDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVV IGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYK SFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLT VTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQ ANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLLRIEEELGSKAKFAGRNFRNPL Description Functional site 1) chain D residue 165 type sequence Q description BINDING SITE FOR RESIDUE MG D 707 source : AC7 2) chain D residue 244 type sequence D description BINDING SITE FOR RESIDUE MG D 707 source : AC7 3) chain D residue 292 type sequence E description BINDING SITE FOR RESIDUE MG D 707 source : AC7 4) chain D residue 317 type sequence D description BINDING SITE FOR RESIDUE MG D 707 source : AC7 5) chain D residue 342 type sequence K description BINDING SITE FOR RESIDUE MG D 707 source : AC7 6) chain D residue 39 type sequence S description BINDING SITE FOR RESIDUE MG D 708 source : AC8 7) chain D residue 317 type sequence D description BINDING SITE FOR RESIDUE MG D 708 source : AC8 8) chain D residue 342 type sequence K description BINDING SITE FOR RESIDUE MG D 708 source : AC8 9) chain D residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 10) chain D residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 11) chain D residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 12) chain D residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 13) chain D residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 14) chain D residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 15) chain D residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 16) chain D residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 17) chain D residue 209 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 18) chain D residue 91 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 19) chain D residue 334 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 20) chain D residue 342 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 21) chain D residue 405 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 22) chain D residue 201 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI11 23) chain D residue 232 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI12 24) chain D residue 253 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 25) chain D 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 26) chain D residue 271 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 27) chain D residue 280 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI16 28) chain D residue 290 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 29) chain D 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 30) chain D residue 342 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 31) chain D residue 39 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 32) chain D residue 244 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 33) chain D residue 157 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 34) chain D residue 166 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 35) chain D residue 292 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 36) chain D residue 317 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 37) chain D residue 369 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 38) chain D residue 393 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 39) chain D residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000269|Ref.14, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI5 40) chain D residue 4 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 41) chain D residue 63 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 42) chain D residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 43) chain D residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 44) chain D residue 192 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 45) chain D residue 198 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 46) chain D residue 255 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 47) chain D residue 284 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 48) chain D residue 26 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 49) chain D residue 43 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 50) chain D residue 286 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 51) chain D residue 59 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 52) chain D residue 88 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 53) chain D residue 227 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 54) chain D residue 419 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links