eF-site ID 1mld-A PDB Code 1mld Chain A 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 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 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 10) chain A residue 10 type CARBOHYD sequence G description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 source Swiss-Prot : SWS_FT_FI10 11) chain A residue 8 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 34 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 94 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 228 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 81 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 17) chain A residue 87 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 18) chain A residue 119 type BINDING sequence P description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 19) chain A residue 153 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 20) chain A residue 180 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 21) chain A residue 246 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 22) chain A residue 216 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 23) chain A residue 278 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 24) chain A residue 305 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 25) chain A residue 223 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 26) chain A residue 303 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 27) chain A residue 306 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI9 28) chain A residue 145-157 type prosite sequence VTTLDIVRANAFV description MDH Malate dehydrogenase active site signature. VTTLDivRAnafV source prosite : PS00068 29) chain A residue 55 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 68 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 31) chain A residue 162 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 32) chain A residue 192 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 273 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 284 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 291 type MOD_RES sequence M description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 301 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 312 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 142 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI5

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