eF-site ID 1egd-A PDB Code 1egd Chain A click to enlarge Title STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE Classification ELECTRON TRANSFER Compound MEDIUM CHAIN ACYL-COA DEHYDROGENASE Source Homo sapiens (Human) (ACADM_HUMAN) Sequence A:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYGGTSQIQRLIVAREHIDKYKN Description Functional site 1) chain A residue 376 type sequence G description CATALYTIC BASE IN CHAIN A source : CA1 2) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 3) chain A residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 4) chain A residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 5) chain A residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 6) chain A residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 7) chain A residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 8) chain A residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 9) chain A residue 214 type sequence N description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 10) chain A residue 371 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 11) chain A residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 12) chain A residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 13) chain A residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 14) chain A residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 15) chain A residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 16) chain A residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 17) chain A residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 18) chain A residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 19) chain A residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 20) chain A residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 21) chain A residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 22) chain A residue 376 type ACT_SITE sequence G description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 133 type BINDING sequence Y description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 166 type BINDING sequence W description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 291 type BINDING sequence H description in other chain => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 27) chain A residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 28) chain A residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 29) chain A residue 376 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 30) chain A residue 134-146 type prosite sequence CVTEPGAGSDVAG description ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CVTEpgAGSDvaG source prosite : PS00072 31) chain A residue 349-368 type prosite sequence QILGGNGFNTEYPVEKLMRD description ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiLGGnGFntEypveKlmrD source prosite : PS00073 32) chain A residue 281 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 33) chain A residue 349 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15159392, ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8823176, ECO:0000269|Ref.23, ECO:0007744|PDB:1EGC, ECO:0007744|PDB:1EGD, ECO:0007744|PDB:1EGE, ECO:0007744|PDB:1T9G, ECO:0007744|PDB:2A1T, ECO:0007744|PDB:4P13 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8 35) chain A residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 36) chain A residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 40) chain A residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 41) chain A residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 42) chain A residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7

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