eF-site ID 2psn-ABCD PDB Code 2psn Chain A, B, C, D 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 B:  SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGAST GIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKK LNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKA GAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGN KLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYG KDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVV IGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYK SFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLT VTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQ ANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLLRIEEELGSKAKFAGRNFRNPLA C:  SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGAST GIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKK LNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKA GAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGN KLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYG KDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVV IGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYK SFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLT VTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQ ANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK D:  SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGAST GIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKK LNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKA GAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGN KLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYG KDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVV IGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYK SFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLT VTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQ ANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS ERLAKYNQLLRIEEELGSKAKFAGRNFRNPL 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 B residue 165 type sequence Q description BINDING SITE FOR RESIDUE MG B 703 source : AC3 10) chain B residue 244 type sequence D description BINDING SITE FOR RESIDUE MG B 703 source : AC3 11) chain B residue 292 type sequence E description BINDING SITE FOR RESIDUE MG B 703 source : AC3 12) chain B residue 317 type sequence D description BINDING SITE FOR RESIDUE MG B 703 source : AC3 13) chain B residue 342 type sequence K description BINDING SITE FOR RESIDUE MG B 703 source : AC3 14) chain B residue 39 type sequence S description BINDING SITE FOR RESIDUE MG B 704 source : AC4 15) chain B residue 317 type sequence D description BINDING SITE FOR RESIDUE MG B 704 source : AC4 16) chain B residue 342 type sequence K description BINDING SITE FOR RESIDUE MG B 704 source : AC4 17) chain C residue 165 type sequence Q description BINDING SITE FOR RESIDUE MG C 705 source : AC5 18) chain C residue 244 type sequence D description BINDING SITE FOR RESIDUE MG C 705 source : AC5 19) chain C residue 292 type sequence E description BINDING SITE FOR RESIDUE MG C 705 source : AC5 20) chain C residue 317 type sequence D description BINDING SITE FOR RESIDUE MG C 705 source : AC5 21) chain C residue 342 type sequence K description BINDING SITE FOR RESIDUE MG C 705 source : AC5 22) chain C residue 39 type sequence S description BINDING SITE FOR RESIDUE MG C 706 source : AC6 23) chain C residue 317 type sequence D description BINDING SITE FOR RESIDUE MG C 706 source : AC6 24) chain C residue 342 type sequence K description BINDING SITE FOR RESIDUE MG C 706 source : AC6 25) chain D residue 165 type sequence Q description BINDING SITE FOR RESIDUE MG D 707 source : AC7 26) chain D residue 244 type sequence D description BINDING SITE FOR RESIDUE MG D 707 source : AC7 27) chain D residue 292 type sequence E description BINDING SITE FOR RESIDUE MG D 707 source : AC7 28) chain D residue 317 type sequence D description BINDING SITE FOR RESIDUE MG D 707 source : AC7 29) chain D residue 342 type sequence K description BINDING SITE FOR RESIDUE MG D 707 source : AC7 30) chain D residue 39 type sequence S description BINDING SITE FOR RESIDUE MG D 708 source : AC8 31) chain D residue 317 type sequence D description BINDING SITE FOR RESIDUE MG D 708 source : AC8 32) chain D residue 342 type sequence K description BINDING SITE FOR RESIDUE MG D 708 source : AC8 33) chain A residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 34) chain A residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 35) chain A residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 36) chain A residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 37) chain A residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 38) chain A residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 39) chain A residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 40) chain A residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 A 709 source : AC9 41) chain B residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 B 710 source : BC1 42) chain B residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 B 710 source : BC1 43) chain B residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 B 710 source : BC1 44) chain B residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 B 710 source : BC1 45) chain B residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 B 710 source : BC1 46) chain B residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 B 710 source : BC1 47) chain B residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 B 710 source : BC1 48) chain B residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 B 710 source : BC1 49) chain C residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 50) chain C residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 51) chain C residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 52) chain C residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 53) chain C residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 54) chain C residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 55) chain C residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 56) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 C 711 source : BC2 57) chain D residue 37 type sequence G description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 58) chain D residue 38 type sequence A description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 59) chain D residue 39 type sequence S description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 60) chain D residue 157 type sequence H description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 61) chain D residue 165 type sequence Q description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 62) chain D residue 342 type sequence K description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 63) chain D residue 371 type sequence R description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 64) chain D residue 372 type sequence S description BINDING SITE FOR RESIDUE PO4 D 712 source : BC3 65) chain A residue 39 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 66) chain A residue 244 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 67) chain B residue 39 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 68) chain B residue 244 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 69) chain C residue 39 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 70) chain C residue 244 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 71) chain D residue 39 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 72) chain D residue 244 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18560153 source Swiss-Prot : SWS_FT_FI3 73) chain A residue 209 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 74) chain B residue 209 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 75) chain C residue 209 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 76) chain D residue 209 type ACT_SITE sequence E description Proton donor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI1 77) chain A residue 342 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 78) chain B residue 342 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 79) chain C residue 342 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 80) chain D residue 342 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI2 81) chain A residue 91 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 82) chain C residue 334 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 83) chain C residue 342 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 84) chain C residue 405 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 85) chain D residue 91 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 86) chain D residue 334 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 87) chain D residue 342 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 88) chain D residue 405 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 89) chain A residue 334 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 90) chain A residue 342 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 91) chain A residue 405 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 92) chain B residue 91 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 93) chain B residue 334 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 94) chain B residue 342 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 95) chain B residue 405 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 96) chain C residue 91 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI10 97) chain A residue 201 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI11 98) chain B residue 201 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI11 99) chain C residue 201 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI11 100) chain D residue 201 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI11 101) 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 102) chain B residue 253 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI13 103) 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 104) 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 105) 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 106) chain B 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 107) 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 108) 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 109) 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 110) chain B residue 271 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI15 111) 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 112) 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 113) chain A residue 339-352 type prosite sequence LLLKVNQIGSVTES description ENOLASE Enolase signature. LLLKvNQIGSVTES source prosite : PS00164 114) chain A residue 232 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI12 115) chain B residue 232 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI12 116) chain C residue 232 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI12 117) chain D residue 232 type MOD_RES sequence K description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771 source Swiss-Prot : SWS_FT_FI12 118) chain A residue 280 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI16 119) chain B residue 280 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI16 120) chain C residue 280 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI16 121) chain D residue 280 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI16 122) chain A residue 290 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 123) chain B residue 290 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 124) chain C residue 290 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 125) chain D residue 290 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI17 126) 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 127) chain B 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 128) 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 129) 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 130) chain A residue 157 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 131) chain B residue 317 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 132) chain B residue 369 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 133) chain B residue 393 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 134) chain C residue 157 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 135) chain C residue 166 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 136) chain C residue 292 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 137) chain C residue 317 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 138) chain C residue 369 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 139) chain C residue 393 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 140) chain D residue 157 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 141) chain A residue 166 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 142) chain D residue 166 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 143) chain D residue 292 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 144) chain D residue 317 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 145) chain D residue 369 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 146) chain D residue 393 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 147) chain A residue 292 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 148) chain A residue 317 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 149) chain A residue 369 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 150) chain A residue 393 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 151) chain B residue 157 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 152) chain B residue 166 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 153) chain B residue 292 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00924 source Swiss-Prot : SWS_FT_FI4 154) 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 155) chain B residue 1 type MOD_RES sequence S description N-acetylserine => ECO:0000269|Ref.14, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI5 156) 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 157) 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 158) chain A residue 4 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 159) chain B residue 63 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 160) chain B residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 161) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 162) chain B residue 192 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 163) chain B residue 198 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 164) chain B residue 255 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 165) chain B residue 284 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 166) chain C residue 4 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 167) chain C residue 63 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 168) chain C residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 169) chain A residue 63 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 170) chain C residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 171) chain C residue 192 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 172) chain C residue 198 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 173) chain C residue 255 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 174) chain C residue 284 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 175) chain D residue 4 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 176) chain D residue 63 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 177) chain D residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 178) chain D residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 179) chain D residue 192 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 180) chain A residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 181) chain D residue 198 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 182) chain D residue 255 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 183) chain D residue 284 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 184) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 185) chain A residue 192 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 186) chain A residue 198 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 187) chain A residue 255 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 188) chain A residue 284 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 189) chain B residue 4 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 190) chain A residue 26 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 191) chain B residue 26 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 192) chain C residue 26 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 193) chain D residue 26 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 194) chain A residue 43 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 195) chain A residue 286 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 196) chain B residue 43 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 197) chain B residue 286 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 198) chain C residue 43 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 199) chain C residue 286 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 200) chain D residue 43 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 201) chain D residue 286 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 202) chain A residue 59 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 203) chain C residue 88 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 204) chain C residue 227 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 205) chain C residue 419 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 206) chain D residue 59 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 207) chain D residue 88 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 208) chain D residue 227 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 209) chain D residue 419 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 210) chain A residue 88 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 211) chain A residue 227 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 212) chain A residue 419 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 213) chain B residue 59 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 214) chain B residue 88 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 215) chain B residue 227 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 216) chain B residue 419 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9 217) chain C residue 59 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 source Swiss-Prot : SWS_FT_FI9

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