eF-site ID 1mld-D PDB Code 1mld Chain 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 null (MDHM_PIG) Sequence D:  AKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGV AADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPR KPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPV NSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANAFVAEL KGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLS TLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVD AMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLG IGKISPFEEKMIAEAIPELKASIKKGEEFVKNM Description Functional site 1) chain D residue 12 type sequence I description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 2) chain D residue 80 type sequence R description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 3) chain D residue 86 type sequence R description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 4) chain D residue 118 type sequence N description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 5) chain D residue 152 type sequence R description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 6) chain D residue 176 type sequence H description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 7) chain D residue 210 type sequence G description BINDING SITE FOR RESIDUE CIT D 375 source : AC4 8) 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 9) chain D residue 8 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 10) chain D residue 34 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 11) chain D residue 94 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 12) chain D residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 13) chain D residue 228 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 14) chain D residue 81 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 15) chain D residue 87 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 16) chain D residue 119 type BINDING sequence P description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 17) chain D residue 153 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 18) chain D residue 55 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 19) chain D residue 68 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 20) chain D residue 162 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 21) chain D residue 192 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 22) chain D residue 273 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 23) chain D residue 284 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 24) chain D residue 291 type MOD_RES sequence M description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 25) chain D residue 301 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 26) chain D residue 312 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 27) chain D residue 142 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI5 28) chain D residue 180 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 29) chain D residue 246 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 30) chain D residue 216 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 31) chain D residue 278 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 32) chain D residue 305 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 33) chain D residue 223 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 34) chain D residue 303 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 35) chain D residue 10 type CARBOHYD sequence G description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 source Swiss-Prot : SWS_FT_FI10 36) chain D 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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