eF-site ID 2vd6-ABCD PDB Code 2vd6 Chain A, B, C, D click to enlarge Title Human adenylosuccinate lyase in complex with its substrate N6-(1,2- Dicarboxyethyl)-AMP, and its products AMP and fumarate. Classification LYASE Compound ADENYLOSUCCINATE LYASE Source Homo sapiens (Human) (PUR8_HUMAN) Sequence A:  GDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWL WLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRL RHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIIL RNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQ LTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGT QASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYT RKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEP YKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDD SANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRI RQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASV VKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRA SQQVQRFLEEEVYPLLKPYES B:  GDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWL WLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRL RHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIIL RNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQ LTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGT QASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYT RKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFYK RNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSA NRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQ ELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVK QEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQ QVQRFLEEEVYPLLKPYESVM C:  GDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWL WLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRL RHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIIL RNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQ LTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGT QASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYT RKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFYK RNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSA NRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQ ELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVK QEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQ QVQRFLEEEVYPLLKPY D:  GDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWL WLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRL RHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIIL RNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQ LTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGT QASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYT RKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFPY KRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDS ANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIR QELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVV KQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRAS QQVQRFLEEEVYPLLKPYESVM Description Functional site 1) chain A residue 85 type sequence R description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 2) chain A residue 86 type sequence H description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 3) chain A residue 87 type sequence D description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 4) chain A residue 112 type sequence S description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 5) chain A residue 241 type sequence Q description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 6) chain A residue 329 type sequence R description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 7) chain A residue 331 type sequence L description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 8) chain A residue 334 type sequence S description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 9) chain A residue 335 type sequence A description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 10) chain A residue 338 type sequence R description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 11) chain B residue 159 type sequence H description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 12) chain D residue 20 type sequence R description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 13) chain D residue 21 type sequence Y description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 14) chain D residue 299 type sequence M description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 15) chain D residue 303 type sequence R description BINDING SITE FOR RESIDUE AMP A 1000 source : AC1 16) chain A residue 86 type sequence H description BINDING SITE FOR RESIDUE FUM A 1001 source : AC2 17) chain A residue 89 type sequence M description BINDING SITE FOR RESIDUE FUM A 1001 source : AC2 18) chain A residue 111 type sequence T description BINDING SITE FOR RESIDUE FUM A 1001 source : AC2 19) chain A residue 112 type sequence S description BINDING SITE FOR RESIDUE FUM A 1001 source : AC2 20) chain A residue 241 type sequence Q description BINDING SITE FOR RESIDUE FUM A 1001 source : AC2 21) chain B residue 158 type sequence T description BINDING SITE FOR RESIDUE FUM A 1001 source : AC2 22) chain B residue 159 type sequence H description BINDING SITE FOR RESIDUE FUM A 1001 source : AC2 23) chain D residue 295 type sequence K description BINDING SITE FOR RESIDUE FUM A 1001 source : AC2 24) chain A residue 35 type sequence K description BINDING SITE FOR RESIDUE GOL A 1003 source : AC3 25) chain A residue 39 type sequence W description BINDING SITE FOR RESIDUE GOL A 1003 source : AC3 26) chain A residue 87 type sequence D description BINDING SITE FOR RESIDUE GOL A 1003 source : AC3 27) chain A residue 116 type sequence G description BINDING SITE FOR RESIDUE GOL A 1003 source : AC3 28) chain A residue 120 type sequence D description BINDING SITE FOR RESIDUE GOL A 1003 source : AC3 29) chain A residue 334 type sequence S description BINDING SITE FOR RESIDUE GOL A 1003 source : AC3 30) chain A residue 338 type sequence R description BINDING SITE FOR RESIDUE GOL A 1003 source : AC3 31) chain D residue 297 type sequence N description BINDING SITE FOR RESIDUE CL A 2001 source : AC4 32) chain D residue 299 type sequence M description BINDING SITE FOR RESIDUE CL A 2001 source : AC4 33) chain A residue 111 type sequence T description BINDING SITE FOR RESIDUE CL A 2002 source : AC5 34) chain A residue 114 type sequence Y description BINDING SITE FOR RESIDUE CL A 2002 source : AC5 35) chain A residue 196 type sequence R description BINDING SITE FOR RESIDUE CL A 2002 source : AC5 36) chain A residue 199 type sequence K description BINDING SITE FOR RESIDUE CL A 2002 source : AC5 37) chain A residue 200 type sequence G description BINDING SITE FOR RESIDUE CL A 2002 source : AC5 38) chain A residue 158 type sequence T description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 39) chain A residue 159 type sequence H description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 40) chain B residue 85 type sequence R description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 41) chain B residue 86 type sequence H description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 42) chain B residue 87 type sequence D description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 43) chain B residue 111 type sequence T description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 44) chain B residue 112 type sequence S description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 45) chain B residue 241 type sequence Q description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 46) chain B residue 329 type sequence R description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 47) chain B residue 334 type sequence S description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 48) chain B residue 335 type sequence A description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 49) chain B residue 338 type sequence R description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 50) chain C residue 20 type sequence R description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 51) chain C residue 21 type sequence Y description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 52) chain C residue 295 type sequence K description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 53) chain C residue 299 type sequence M description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 54) chain C residue 303 type sequence R description BINDING SITE FOR RESIDUE 2SA B 1002 source : AC6 55) chain B residue 35 type sequence K description BINDING SITE FOR RESIDUE GOL B 1003 source : AC7 56) chain B residue 87 type sequence D description BINDING SITE FOR RESIDUE GOL B 1003 source : AC7 57) chain B residue 116 type sequence G description BINDING SITE FOR RESIDUE GOL B 1003 source : AC7 58) chain B residue 120 type sequence D description BINDING SITE FOR RESIDUE GOL B 1003 source : AC7 59) chain B residue 334 type sequence S description BINDING SITE FOR RESIDUE GOL B 1003 source : AC7 60) chain B residue 338 type sequence R description BINDING SITE FOR RESIDUE GOL B 1003 source : AC7 61) chain B residue 120 type sequence D description BINDING SITE FOR RESIDUE GOL B 1004 source : AC8 62) chain B residue 337 type sequence R description BINDING SITE FOR RESIDUE GOL B 1004 source : AC8 63) chain B residue 338 type sequence R description BINDING SITE FOR RESIDUE GOL B 1004 source : AC8 64) chain B residue 341 type sequence L description BINDING SITE FOR RESIDUE GOL B 1004 source : AC8 65) chain B residue 342 type sequence A description BINDING SITE FOR RESIDUE GOL B 1004 source : AC8 66) chain C residue 297 type sequence N description BINDING SITE FOR RESIDUE CL B 2001 source : AC9 67) chain B residue 111 type sequence T description BINDING SITE FOR RESIDUE CL B 2002 source : BC1 68) chain B residue 114 type sequence Y description BINDING SITE FOR RESIDUE CL B 2002 source : BC1 69) chain B residue 196 type sequence R description BINDING SITE FOR RESIDUE CL B 2002 source : BC1 70) chain B residue 199 type sequence K description BINDING SITE FOR RESIDUE CL B 2002 source : BC1 71) chain B residue 200 type sequence G description BINDING SITE FOR RESIDUE CL B 2002 source : BC1 72) chain B residue 20 type sequence R description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 73) chain B residue 21 type sequence Y description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 74) chain B residue 299 type sequence M description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 75) chain B residue 303 type sequence R description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 76) chain C residue 85 type sequence R description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 77) chain C residue 86 type sequence H description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 78) chain C residue 87 type sequence D description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 79) chain C residue 112 type sequence S description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 80) chain C residue 241 type sequence Q description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 81) chain C residue 329 type sequence R description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 82) chain C residue 331 type sequence L description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 83) chain C residue 334 type sequence S description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 84) chain C residue 335 type sequence A description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 85) chain C residue 338 type sequence R description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 86) chain D residue 159 type sequence H description BINDING SITE FOR RESIDUE AMP C 1000 source : BC2 87) chain B residue 295 type sequence K description BINDING SITE FOR RESIDUE FUM C 1001 source : BC3 88) chain B residue 297 type sequence N description BINDING SITE FOR RESIDUE FUM C 1001 source : BC3 89) chain C residue 86 type sequence H description BINDING SITE FOR RESIDUE FUM C 1001 source : BC3 90) chain C residue 111 type sequence T description BINDING SITE FOR RESIDUE FUM C 1001 source : BC3 91) chain C residue 112 type sequence S description BINDING SITE FOR RESIDUE FUM C 1001 source : BC3 92) chain C residue 241 type sequence Q description BINDING SITE FOR RESIDUE FUM C 1001 source : BC3 93) chain D residue 158 type sequence T description BINDING SITE FOR RESIDUE FUM C 1001 source : BC3 94) chain D residue 159 type sequence H description BINDING SITE FOR RESIDUE FUM C 1001 source : BC3 95) chain C residue 35 type sequence K description BINDING SITE FOR RESIDUE GOL C 1003 source : BC4 96) chain C residue 39 type sequence W description BINDING SITE FOR RESIDUE GOL C 1003 source : BC4 97) chain C residue 87 type sequence D description BINDING SITE FOR RESIDUE GOL C 1003 source : BC4 98) chain C residue 116 type sequence G description BINDING SITE FOR RESIDUE GOL C 1003 source : BC4 99) chain C residue 120 type sequence D description BINDING SITE FOR RESIDUE GOL C 1003 source : BC4 100) chain C residue 334 type sequence S description BINDING SITE FOR RESIDUE GOL C 1003 source : BC4 101) chain C residue 338 type sequence R description BINDING SITE FOR RESIDUE GOL C 1003 source : BC4 102) chain C residue 114 type sequence Y description BINDING SITE FOR RESIDUE CL C 2002 source : BC5 103) chain C residue 196 type sequence R description BINDING SITE FOR RESIDUE CL C 2002 source : BC5 104) chain C residue 199 type sequence K description BINDING SITE FOR RESIDUE CL C 2002 source : BC5 105) chain C residue 200 type sequence G description BINDING SITE FOR RESIDUE CL C 2002 source : BC5 106) chain A residue 20 type sequence R description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 107) chain A residue 21 type sequence Y description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 108) chain A residue 295 type sequence K description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 109) chain A residue 299 type sequence M description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 110) chain A residue 303 type sequence R description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 111) chain C residue 158 type sequence T description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 112) chain C residue 159 type sequence H description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 113) chain D residue 85 type sequence R description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 114) chain D residue 86 type sequence H description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 115) chain D residue 87 type sequence D description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 116) chain D residue 111 type sequence T description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 117) chain D residue 112 type sequence S description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 118) chain D residue 241 type sequence Q description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 119) chain D residue 329 type sequence R description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 120) chain D residue 334 type sequence S description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 121) chain D residue 335 type sequence A description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 122) chain D residue 338 type sequence R description BINDING SITE FOR RESIDUE 2SA D 1002 source : BC6 123) chain D residue 35 type sequence K description BINDING SITE FOR RESIDUE GOL D 1003 source : BC7 124) chain D residue 39 type sequence W description BINDING SITE FOR RESIDUE GOL D 1003 source : BC7 125) chain D residue 87 type sequence D description BINDING SITE FOR RESIDUE GOL D 1003 source : BC7 126) chain D residue 116 type sequence G description BINDING SITE FOR RESIDUE GOL D 1003 source : BC7 127) chain D residue 120 type sequence D description BINDING SITE FOR RESIDUE GOL D 1003 source : BC7 128) chain D residue 334 type sequence S description BINDING SITE FOR RESIDUE GOL D 1003 source : BC7 129) chain D residue 338 type sequence R description BINDING SITE FOR RESIDUE GOL D 1003 source : BC7 130) chain A residue 297 type sequence N description BINDING SITE FOR RESIDUE CL D 2001 source : BC8 131) chain A residue 299 type sequence M description BINDING SITE FOR RESIDUE CL D 2001 source : BC8 132) chain D residue 111 type sequence T description BINDING SITE FOR RESIDUE CL D 2002 source : BC9 133) chain D residue 114 type sequence Y description BINDING SITE FOR RESIDUE CL D 2002 source : BC9 134) chain D residue 196 type sequence R description BINDING SITE FOR RESIDUE CL D 2002 source : BC9 135) chain D residue 199 type sequence K description BINDING SITE FOR RESIDUE CL D 2002 source : BC9 136) chain D residue 200 type sequence G description BINDING SITE FOR RESIDUE CL D 2002 source : BC9 137) chain A residue 415 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI6 138) chain B residue 415 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI6 139) chain C residue 415 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI6 140) chain D residue 415 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI6 141) chain A residue 20 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 142) chain A residue 303 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 143) chain B residue 20 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 144) chain B residue 303 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 145) chain C residue 20 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 146) chain C residue 303 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 147) chain D residue 20 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 148) chain D residue 303 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 149) chain A residue 85 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 150) chain B residue 329 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 151) chain B residue 334 type BINDING sequence S description in other chain source Swiss-Prot : SWS_FT_FI3 152) chain B residue 338 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 153) chain C residue 85 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 154) chain C residue 111 type BINDING sequence T description in other chain source Swiss-Prot : SWS_FT_FI3 155) chain C residue 241 type BINDING sequence Q description in other chain source Swiss-Prot : SWS_FT_FI3 156) chain C residue 329 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 157) chain C residue 334 type BINDING sequence S description in other chain source Swiss-Prot : SWS_FT_FI3 158) chain C residue 338 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 159) chain D residue 85 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 160) chain A residue 111 type BINDING sequence T description in other chain source Swiss-Prot : SWS_FT_FI3 161) chain D residue 111 type BINDING sequence T description in other chain source Swiss-Prot : SWS_FT_FI3 162) chain D residue 241 type BINDING sequence Q description in other chain source Swiss-Prot : SWS_FT_FI3 163) chain D residue 329 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 164) chain D residue 334 type BINDING sequence S description in other chain source Swiss-Prot : SWS_FT_FI3 165) chain D residue 338 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 166) chain A residue 241 type BINDING sequence Q description in other chain source Swiss-Prot : SWS_FT_FI3 167) chain A residue 329 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 168) chain A residue 334 type BINDING sequence S description in other chain source Swiss-Prot : SWS_FT_FI3 169) chain A residue 338 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 170) chain B residue 85 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 171) chain B residue 111 type BINDING sequence T description in other chain source Swiss-Prot : SWS_FT_FI3 172) chain B residue 241 type BINDING sequence Q description in other chain source Swiss-Prot : SWS_FT_FI3 173) chain A residue 159 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000269|PubMed:22812634 source Swiss-Prot : SWS_FT_FI1 174) chain B residue 159 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000269|PubMed:22812634 source Swiss-Prot : SWS_FT_FI1 175) chain C residue 159 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000269|PubMed:22812634 source Swiss-Prot : SWS_FT_FI1 176) chain D residue 159 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000269|PubMed:22812634 source Swiss-Prot : SWS_FT_FI1 177) chain A residue 147 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 178) chain A residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 179) chain B residue 147 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 180) chain B residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 181) chain C residue 147 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 182) chain C residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 183) chain D residue 147 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 184) chain D residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5

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