eF-site ID 1mld-ABCD PDB Code 1mld Chain A, B, C, D click to enlarge Title REFINED STRUCTURE OF MITOCHONDRIAL MALATE DEHYDROGENASE FROM PORCINE HEART AND THE CONSENSUS STRUCTURE FOR DICARBOXYLIC ACID OXIDOREDUCTASES Classification OXIDOREDUCTASE(NAD(A)-CHOH(D)) Compound MALATE DEHYDROGENASE Source Sus scrofa (Pig) (MDHM_PIG) Sequence A:  AKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGV AADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPR KPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPV NSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANAFVAEL KGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLS TLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVD AMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLG IGKISPFEEKMIAEAIPELKASIKKGEEFVKNM B:  AKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGV AADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPR KPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPV NSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANAFVAEL KGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLS TLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVD AMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLG IGKISPFEEKMIAEAIPELKASIKKGEEFVKNM C:  AKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGV AADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPR KPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPV NSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANAFVAEL KGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLS TLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVD AMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLG IGKISPFEEKMIAEAIPELKASIKKGEEFVKNM D:  AKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGV AADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPR KPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPV NSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANAFVAEL KGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLS TLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVD AMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLG IGKISPFEEKMIAEAIPELKASIKKGEEFVKNM Description Functional site 1) chain A residue 12 type sequence I description BINDING SITE FOR RESIDUE CIT A 375 source : AC1 2) chain A residue 80 type sequence R description BINDING SITE FOR RESIDUE CIT A 375 source : AC1 3) chain A residue 86 type sequence R description BINDING SITE FOR RESIDUE CIT A 375 source : AC1 4) chain A residue 118 type sequence N description BINDING SITE FOR RESIDUE CIT A 375 source : AC1 5) chain A residue 152 type sequence R description BINDING SITE FOR RESIDUE CIT A 375 source : AC1 6) chain A residue 176 type sequence H description BINDING SITE FOR RESIDUE CIT A 375 source : AC1 7) chain A residue 210 type sequence G description BINDING SITE FOR RESIDUE CIT A 375 source : AC1 8) chain A residue 223 type sequence A description BINDING SITE FOR RESIDUE CIT A 375 source : AC1 9) chain B residue 12 type sequence I description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 10) chain B residue 80 type sequence R description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 11) chain B residue 86 type sequence R description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 12) chain B residue 118 type sequence N description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 13) chain B residue 148 type sequence L description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 14) chain B residue 152 type sequence R description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 15) chain B residue 176 type sequence H description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 16) chain B residue 210 type sequence G description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 17) chain B residue 223 type sequence A description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 18) chain B residue 227 type sequence M description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 19) chain C residue 12 type sequence I description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 20) chain C residue 80 type sequence R description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 21) chain C residue 86 type sequence R description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 22) chain C residue 118 type sequence N description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 23) chain C residue 152 type sequence R description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 24) chain C residue 176 type sequence H description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 25) chain C residue 210 type sequence G description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 26) chain C residue 223 type sequence A description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 27) chain C residue 227 type sequence M description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 28) chain D residue 12 type sequence I description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 29) chain D residue 80 type sequence R description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 30) chain D residue 86 type sequence R description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 31) chain D residue 118 type sequence N description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 32) chain D residue 152 type sequence R description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 33) chain D residue 176 type sequence H description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 34) chain D residue 210 type sequence G description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 35) chain A residue 177 type ACT_SITE sequence A description Proton acceptor => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI1 36) chain B residue 177 type ACT_SITE sequence A description Proton acceptor => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI1 37) chain C residue 177 type ACT_SITE sequence A description Proton acceptor => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI1 38) chain D residue 177 type ACT_SITE sequence A description Proton acceptor => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI1 39) chain A residue 10 type CARBOHYD sequence G description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 source Swiss-Prot : SWS_FT_FI10 40) chain B residue 10 type CARBOHYD sequence G description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 source Swiss-Prot : SWS_FT_FI10 41) chain C residue 10 type CARBOHYD sequence G description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 source Swiss-Prot : SWS_FT_FI10 42) chain D residue 10 type CARBOHYD sequence G description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 source Swiss-Prot : SWS_FT_FI10 43) chain A residue 8 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 228 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 45) chain C residue 8 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 46) chain C residue 34 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 47) chain C residue 94 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 48) chain C residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 49) chain C residue 228 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 50) chain D residue 8 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 51) chain D residue 34 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 52) chain D residue 94 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 53) chain D residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 34 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 55) chain D residue 228 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 94 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 228 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 59) chain B residue 8 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 60) chain B residue 34 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 61) chain B residue 94 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 81 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 64) chain C residue 87 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 65) chain C residue 119 type BINDING sequence P description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 66) chain C residue 153 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 67) chain D residue 81 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 68) chain D residue 87 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 69) chain D residue 119 type BINDING sequence P description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 70) chain D residue 153 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 71) chain A residue 87 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 72) chain A residue 119 type BINDING sequence P description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 73) chain A residue 153 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 74) chain B residue 81 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 75) chain B residue 87 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 76) chain B residue 119 type BINDING sequence P description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 77) chain B residue 153 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 78) chain C residue 81 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 79) chain A residue 180 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 80) chain A residue 246 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 81) chain B residue 180 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 82) chain B residue 246 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 83) chain C residue 180 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 84) chain C residue 246 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 85) chain D residue 180 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 86) chain D residue 246 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 87) chain A residue 216 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 88) chain D residue 216 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 89) chain D residue 278 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 90) chain D residue 305 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 91) chain A residue 278 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 92) chain A residue 305 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 93) chain B residue 216 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 94) chain B residue 278 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 95) chain B residue 305 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 96) chain C residue 216 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 97) chain C residue 278 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 98) chain C residue 305 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 99) chain A residue 223 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 100) chain A residue 303 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 101) chain B residue 223 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 102) chain B residue 303 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 103) chain C residue 223 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 104) chain C residue 303 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 105) chain D residue 223 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 106) chain D residue 303 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 107) chain A residue 306 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI9 108) chain B residue 306 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI9 109) chain C residue 306 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI9 110) chain D residue 306 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI9 111) chain A residue 145-157 type prosite sequence VTTLDIVRANAFV description MDH Malate dehydrogenase active site signature. VTTLDivRAnafV source prosite : PS00068 112) chain A residue 55 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 113) chain B residue 55 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 114) chain B residue 68 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 115) chain B residue 162 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 116) chain B residue 192 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 117) chain B residue 273 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 118) chain B residue 284 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 119) chain B residue 291 type MOD_RES sequence M description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 120) chain B residue 301 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 121) chain B residue 312 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 122) chain C residue 55 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 123) chain A residue 68 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 124) chain C residue 68 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 125) chain C residue 162 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 126) chain C residue 192 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 127) chain C residue 273 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 128) chain C residue 284 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 129) chain C residue 291 type MOD_RES sequence M description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 130) chain C residue 301 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 131) chain C residue 312 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 132) chain D residue 55 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 133) chain D residue 68 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 134) chain A residue 162 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 135) chain D residue 162 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 136) chain D residue 192 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 137) chain D residue 273 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 138) chain D residue 284 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 139) chain D residue 291 type MOD_RES sequence M description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 140) chain D residue 301 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 141) chain D residue 312 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 142) chain A residue 192 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 143) chain A residue 273 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 144) chain A residue 284 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 145) chain A residue 291 type MOD_RES sequence M description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 146) chain A residue 301 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 147) chain A residue 312 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 148) chain A residue 142 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI5 149) chain B residue 142 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI5 150) chain C residue 142 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI5 151) chain D residue 142 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI5

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