eF-site ID 1mld-B PDB Code 1mld Chain B 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 B:  AKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGV AADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPR KPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPV NSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANAFVAEL KGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLS TLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVD AMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLG IGKISPFEEKMIAEAIPELKASIKKGEEFVKNM Description Functional site 1) chain B residue 12 type sequence I description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 2) chain B residue 80 type sequence R description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 3) chain B residue 86 type sequence R description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 4) chain B residue 118 type sequence N description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 5) chain B residue 148 type sequence L description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 6) chain B residue 152 type sequence R description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 7) chain B residue 176 type sequence H description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 8) chain B residue 210 type sequence G description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 9) chain B residue 223 type sequence A description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 10) chain B residue 227 type sequence M description BINDING SITE FOR RESIDUE CIT B 375 source : AC2 11) 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 12) chain B residue 10 type CARBOHYD sequence G description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 source Swiss-Prot : SWS_FT_FI10 13) chain B residue 228 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 8 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 34 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 94 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 81 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 19) chain B residue 87 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 20) chain B residue 119 type BINDING sequence P description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 21) chain B residue 153 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 22) chain B residue 55 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 68 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 162 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 192 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 26) chain B residue 273 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 27) chain B residue 284 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 291 type MOD_RES sequence M description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 301 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 30) chain B residue 312 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 31) chain B residue 142 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 180 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 33) chain B residue 246 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 34) chain B residue 216 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 35) chain B residue 278 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 36) chain B residue 305 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 37) chain B residue 223 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 38) chain B residue 303 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 39) chain B residue 306 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI9

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