eF-site ID 1egc-C PDB Code 1egc Chain C click to enlarge Title STRUCTURE OF T255E, E376G MUTANT OF HUMAN MEDIUM CHAIN ACYL-COA DEHYDROGENASE COMPLEXED WITH OCTANOYL-COA Classification ELECTRON TRANSFER Compound MEDIUM CHAIN ACYL-COA DEHYDROGENASE Source Homo sapiens (Human) (ACADM_HUMAN) Sequence C:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYGGTSQIQRLIVAREHIDKYKN Description Functional site 1) chain C residue 255 type sequence E description CATALYTIC BASE IN CHAIN C source : CA3 2) chain C residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 3) chain C residue 192 type sequence K description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 4) chain C residue 99 type sequence E description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 5) chain C residue 100 type sequence G description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 6) chain C residue 103 type sequence L description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 7) chain C residue 136 type sequence T description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 8) chain C residue 142 type sequence S description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 9) chain C residue 144 type sequence V description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 10) chain C residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 11) chain C residue 245 type sequence F description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 12) chain C residue 249 type sequence M description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 13) chain C residue 252 type sequence F description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 14) chain C residue 253 type sequence D description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 15) chain C residue 259 type sequence V description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 16) chain C residue 326 type sequence T description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 17) chain C residue 375 type sequence Y description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 18) chain C residue 376 type sequence G description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 19) chain C residue 377 type sequence G description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 20) chain C residue 388 type sequence R description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 21) chain C residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 22) chain C residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 23) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 24) chain C residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 25) chain C residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 26) chain C residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 27) chain C residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 28) chain C residue 167 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 29) chain C residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 30) chain C residue 214 type sequence N description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 31) chain C residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 32) chain C residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 33) chain C residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 34) chain C residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 35) chain C residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 36) chain C residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 37) chain C residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 38) chain C residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 39) chain C residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 40) chain C residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 41) chain C residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 42) chain C residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 43) chain C residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 44) chain C residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 45) chain C residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 46) chain C residue 376 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 47) chain C residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 48) chain C residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 49) chain C residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 50) chain C residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 51) chain C residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 52) chain C residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 53) chain C 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 54) chain C 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 55) chain C 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 56) chain C residue 376 type ACT_SITE sequence G description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 57) chain C 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 58) chain C 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 59) chain C residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 60) chain C residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 61) chain C residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 62) chain C residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8

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