eF-site ID 2psn-C PDB Code 2psn Chain C click to enlarge Title Crystal structure of enolase1 Classification LYASE Compound Alpha-enolase Source null (ENOA_HUMAN) Sequence C:  SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGAST GIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKK LNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKA GAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGN KLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYG KDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVV IGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYK SFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLT VTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQ ANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK Description Functional site 1) chain C residue 165 type sequence Q description BINDING SITE FOR RESIDUE MG C 705 source : AC5 2) chain C residue 244 type sequence D description BINDING SITE FOR RESIDUE MG C 705 source : AC5 3) chain C residue 292 type sequence E description BINDING SITE FOR RESIDUE MG C 705 source : AC5 4) chain C residue 317 type sequence D description BINDING SITE FOR RESIDUE MG C 705 source : AC5 5) chain C residue 342 type sequence K description BINDING SITE FOR RESIDUE MG C 705 source : AC5 6) chain C residue 39 type sequence S description BINDING SITE FOR RESIDUE MG C 706 source : AC6 7) chain C residue 317 type sequence D description BINDING SITE FOR RESIDUE MG C 706 source : AC6 8) chain C residue 342 type sequence K description BINDING SITE FOR RESIDUE MG C 706 source : AC6 9) chain C residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 10) chain C residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 11) chain C residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 12) chain C residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 13) chain C residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 14) chain C residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 15) chain C residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 16) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 17) chain C residue 209 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 342 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 19) chain C residue 39 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 20) chain C residue 244 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 21) chain C residue 157 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 22) chain C residue 166 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 23) chain C residue 292 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 24) chain C residue 317 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 25) chain C residue 369 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 26) chain C residue 393 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 27) chain C residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000269|Ref.14, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI5 28) chain C residue 4 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 29) chain C residue 63 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 30) chain C residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 31) chain C residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 32) chain C residue 192 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 33) chain C residue 198 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 34) chain C residue 255 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 35) chain C residue 284 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 36) chain C residue 91 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 37) chain C residue 334 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 38) chain C residue 342 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 39) chain C residue 405 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 40) chain C residue 201 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI11 41) chain C residue 232 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI12 42) chain C residue 253 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 43) chain C 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 44) chain C residue 271 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 45) chain C residue 280 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI16 46) chain C residue 290 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 47) chain C residue 26 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 48) chain C 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 49) chain C residue 43 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 50) chain C residue 286 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 51) chain C residue 59 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 52) chain C residue 88 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 53) chain C residue 227 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 54) chain C 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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