eF-site ID 4r68-ABCD PDB Code 4r68 Chain A, B, C, D click to enlarge Title Lactate Dehydrogenase in complex with inhibitor compound 31 Classification OXIDOREDUCTASE Compound L-lactate dehydrogenase A chain Source Homo sapiens (Human) (LDHA_HUMAN) Sequence A:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD TLWGIQKELQF B:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD TLWGIQKELQF C:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK DYNVTANSKLVIITAGALNLVQRNVNIFKFIIPNVVKYSP NCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSAR FRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGV SLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTS WAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFL SVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKE LQF D:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD TLWGIQKELQF Description Functional site 1) chain A residue 28 type sequence G description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 2) chain A residue 29 type sequence A description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 3) chain A residue 30 type sequence V description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 4) chain A residue 51 type sequence D description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 5) chain A residue 52 type sequence V description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 6) chain A residue 53 type sequence I description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 7) chain A residue 94 type sequence T description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 8) chain A residue 95 type sequence A description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 9) chain A residue 96 type sequence G description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 10) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 11) chain A residue 115 type sequence I description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 12) chain A residue 135 type sequence V description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 13) chain A residue 137 type sequence N description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 14) chain A residue 192 type sequence H description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 15) chain A residue 247 type sequence T description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 16) chain A residue 147 type sequence W description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 17) chain A residue 151 type sequence G description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 18) chain A residue 152 type sequence F description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 19) chain A residue 153 type sequence P description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 20) chain A residue 154 type sequence K description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 21) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 22) chain A residue 108 type sequence L description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 23) chain A residue 137 type sequence N description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 24) chain A residue 164 type sequence L description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 25) chain A residue 165 type sequence D description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 26) chain A residue 168 type sequence R description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 27) chain A residue 192 type sequence H description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 28) chain A residue 193 type sequence G description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 29) chain A residue 194 type sequence D description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 30) chain A residue 237 type sequence A description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 31) chain A residue 238 type sequence Y description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 32) chain A residue 241 type sequence I description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 33) chain A residue 247 type sequence T description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 34) chain B residue 28 type sequence G description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 35) chain B residue 29 type sequence A description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 36) chain B residue 30 type sequence V description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 37) chain B residue 51 type sequence D description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 38) chain B residue 53 type sequence I description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 39) chain B residue 94 type sequence T description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 40) chain B residue 95 type sequence A description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 41) chain B residue 96 type sequence G description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 42) chain B residue 98 type sequence R description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 43) chain B residue 115 type sequence I description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 44) chain B residue 119 type sequence I description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 45) chain B residue 135 type sequence V description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 46) chain B residue 137 type sequence N description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 47) chain B residue 192 type sequence H description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 48) chain B residue 247 type sequence T description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 49) chain B residue 251 type sequence I description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 50) chain D residue 102 type sequence G description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 51) chain A residue 283 type sequence K description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 52) chain B residue 147 type sequence W description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 53) chain B residue 151 type sequence G description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 54) chain B residue 153 type sequence P description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 55) chain B residue 154 type sequence K description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 56) chain B residue 105 type sequence R description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 57) chain B residue 108 type sequence L description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 58) chain B residue 137 type sequence N description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 59) chain B residue 164 type sequence L description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 60) chain B residue 165 type sequence D description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 61) chain B residue 168 type sequence R description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 62) chain B residue 192 type sequence H description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 63) chain B residue 193 type sequence G description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 64) chain B residue 194 type sequence D description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 65) chain B residue 237 type sequence A description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 66) chain B residue 238 type sequence Y description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 67) chain B residue 241 type sequence I description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 68) chain B residue 247 type sequence T description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 69) chain C residue 28 type sequence G description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 70) chain C residue 29 type sequence A description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 71) chain C residue 30 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 72) chain C residue 51 type sequence D description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 73) chain C residue 52 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 74) chain C residue 53 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 75) chain C residue 94 type sequence T description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 76) chain C residue 95 type sequence A description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 77) chain C residue 96 type sequence G description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 78) chain C residue 115 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 79) chain C residue 119 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 80) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 81) chain C residue 137 type sequence N description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 82) chain C residue 192 type sequence H description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 83) chain C residue 247 type sequence T description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 84) chain C residue 251 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 85) chain C residue 147 type sequence W description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 86) chain C residue 151 type sequence G description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 87) chain C residue 152 type sequence F description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 88) chain C residue 153 type sequence P description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 89) chain C residue 154 type sequence K description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 90) chain C residue 137 type sequence N description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 91) chain C residue 165 type sequence D description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 92) chain C residue 168 type sequence R description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 93) chain C residue 192 type sequence H description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 94) chain C residue 193 type sequence G description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 95) chain C residue 194 type sequence D description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 96) chain C residue 237 type sequence A description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 97) chain C residue 238 type sequence Y description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 98) chain C residue 241 type sequence I description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 99) chain C residue 247 type sequence T description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 100) chain D residue 28 type sequence G description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 101) chain D residue 29 type sequence A description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 102) chain D residue 30 type sequence V description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 103) chain D residue 51 type sequence D description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 104) chain D residue 52 type sequence V description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 105) chain D residue 53 type sequence I description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 106) chain D residue 94 type sequence T description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 107) chain D residue 95 type sequence A description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 108) chain D residue 96 type sequence G description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 109) chain D residue 118 type sequence F description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 110) chain D residue 119 type sequence I description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 111) chain D residue 135 type sequence V description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 112) chain D residue 137 type sequence N description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 113) chain D residue 192 type sequence H description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 114) chain D residue 247 type sequence T description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 115) chain D residue 251 type sequence I description BINDING SITE FOR RESIDUE NAI D 801 source : BC1 116) chain D residue 99 type sequence Q description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 117) chain D residue 108 type sequence L description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 118) chain D residue 137 type sequence N description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 119) chain D residue 164 type sequence L description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 120) chain D residue 165 type sequence D description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 121) chain D residue 168 type sequence R description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 122) chain D residue 192 type sequence H description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 123) chain D residue 193 type sequence G description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 124) chain D residue 194 type sequence D description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 125) chain D residue 237 type sequence A description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 126) chain D residue 238 type sequence Y description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 127) chain D residue 241 type sequence I description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 128) chain D residue 247 type sequence T description BINDING SITE FOR RESIDUE W31 D 802 source : BC2 129) chain A residue 242 type sequence K description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 130) chain A residue 243 type sequence L description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 131) chain A residue 244 type sequence K description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 132) chain A residue 245 type sequence G description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 133) chain B residue 55 type sequence D description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 134) chain B residue 56 type sequence K description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 135) chain D residue 97 type sequence A description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 136) chain D residue 98 type sequence R description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 137) chain D residue 103 type sequence E description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 138) chain D residue 111 type sequence R description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 139) chain B residue 185 type sequence H description BINDING SITE FOR RESIDUE SO4 D 804 source : BC4 140) chain D residue 170 type sequence R description BINDING SITE FOR RESIDUE SO4 D 804 source : BC4 141) chain D residue 185 type sequence H description BINDING SITE FOR RESIDUE SO4 D 804 source : BC4 142) chain A residue 189-195 type prosite sequence LGEHGDS description L_LDH L-lactate dehydrogenase active site. LGEHGDS source prosite : PS00064 143) chain A residue 192 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 144) chain B residue 192 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 145) chain C residue 192 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 146) chain D residue 192 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 147) chain A residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 148) chain D residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 149) chain D residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 150) chain D residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 151) chain A residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 152) chain A residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 153) chain B residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 154) chain B residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 155) chain B residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 156) chain C residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 157) chain C residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 158) chain C residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 159) chain A residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI11 160) chain B residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI11 161) chain C residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI11 162) chain D residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI11 163) chain A residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 164) chain A residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 165) chain B residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 166) chain B residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 167) chain C residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 168) chain C residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 169) chain D residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 170) chain D residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 171) chain A residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 172) chain B residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 173) chain C residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 174) chain D residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 175) chain A residue 56 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_FI14 176) chain B residue 56 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_FI14 177) chain C residue 56 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_FI14 178) chain D residue 56 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_FI14 179) chain A residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 180) chain A residue 98 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 181) chain B residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 182) chain B residue 98 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 183) chain C residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 184) chain D residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 185) chain D residue 98 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 186) chain A residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 187) chain C residue 137 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 188) chain C residue 168 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 189) chain C residue 247 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 190) chain D residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 191) chain D residue 137 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 192) chain D residue 168 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 193) chain D residue 247 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 194) chain A residue 137 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 195) chain A residue 168 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 196) chain A residue 247 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 197) chain B residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 198) chain B residue 137 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 199) chain B residue 168 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 200) chain B residue 247 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 201) chain A residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 source Swiss-Prot : SWS_FT_FI4 202) chain B residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 source Swiss-Prot : SWS_FT_FI4 203) chain C residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 source Swiss-Prot : SWS_FT_FI4 204) chain D residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 source Swiss-Prot : SWS_FT_FI4 205) chain A residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 206) chain D residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 207) chain D residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 208) chain D residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 209) chain A residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 210) chain A residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 211) chain B residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 212) chain B residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 213) chain B residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 214) chain C residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 215) chain C residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 216) chain C residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 217) chain A residue 9 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI6 218) chain B residue 9 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI6 219) chain C residue 9 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI6 220) chain D residue 9 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI6 221) chain A residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 222) chain D residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 223) chain D residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 224) chain D residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 225) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 226) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 227) chain B residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 228) chain B residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 229) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 230) chain C residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 231) chain C residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 232) chain C residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 233) chain A residue 17 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 234) chain B residue 17 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 235) chain C residue 17 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 236) chain D residue 17 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 237) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 238) chain B residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 239) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 240) chain D residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9

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