eF-site ID 1mld-C PDB Code 1mld Chain C 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 C:  AKVAVLGASGGIGQPLSLLLKNSPLVSRLTLYDIAHTPGV AADLSHIETRATVKGYLGPEQLPDCLKGCDVVVIPAGVPR KPGMTRDDLFNTNATIVATLTAACAQHCPDAMICIISNPV NSTIPITAEVFKKHGVYNPNKIFGVTTLDIVRANAFVAEL KGLDPARVSVPVIGGHAGKTIIPLISQCTPKVDFPQDQLS TLTGRIQEAGTEVVKAKAGAGSATLSMAYAGARFVFSLVD AMNGKEGVVECSFVKSQETDCPYFSTPLLLGKKGIEKNLG IGKISPFEEKMIAEAIPELKASIKKGEEFVKNM Description Functional site 1) chain C residue 12 type sequence I description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 2) chain C residue 80 type sequence R description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 3) chain C residue 86 type sequence R description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 4) chain C residue 118 type sequence N description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 5) chain C residue 152 type sequence R description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 6) chain C residue 176 type sequence H description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 7) chain C residue 210 type sequence G description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 8) chain C residue 223 type sequence A description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 9) chain C residue 227 type sequence M description BINDING SITE FOR RESIDUE CIT C 375 source : AC3 10) 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 11) chain C residue 10 type CARBOHYD sequence G description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P04636 source Swiss-Prot : SWS_FT_FI10 12) chain C residue 8 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 13) chain C residue 34 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 14) chain C residue 94 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 15) chain C residue 117 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 16) chain C residue 228 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI2 17) chain C residue 87 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 18) chain C residue 119 type BINDING sequence P description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 19) chain C residue 153 type BINDING sequence A description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 20) chain C residue 81 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8117664, ECO:0007744|PDB:1MLD source Swiss-Prot : SWS_FT_FI3 21) chain C residue 180 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 22) chain C residue 246 type MOD_RES sequence E description N6-succinyllysine => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI6 23) chain C residue 216 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 24) chain C residue 278 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 25) chain C residue 305 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI7 26) chain C residue 223 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 27) chain C residue 303 type MOD_RES sequence I description Phosphoserine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI8 28) chain C residue 306 type MOD_RES sequence G description N6-malonyllysine; alternate => ECO:0000250|UniProtKB:Q32LG3 source Swiss-Prot : SWS_FT_FI9 29) chain C residue 55 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 30) chain C residue 68 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 31) chain C residue 162 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 32) chain C residue 192 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 33) chain C residue 273 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 34) chain C residue 284 type MOD_RES sequence I description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 35) chain C residue 291 type MOD_RES sequence M description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 36) chain C residue 301 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 37) chain C residue 312 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08249 source Swiss-Prot : SWS_FT_FI4 38) chain C residue 142 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P40926 source Swiss-Prot : SWS_FT_FI5

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