eF-site ID 1egc-D PDB Code 1egc Chain D 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 null (ACADM_HUMAN) Sequence D:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYGGTSQIQRLIVAREHIDKYKN Description Functional site 1) chain D residue 255 type sequence E description CATALYTIC BASE IN CHAIN D source : CA4 2) chain D residue 95 type sequence Q description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 3) chain D residue 96 type sequence T description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 4) chain D residue 103 type sequence L description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 5) chain D residue 141 type sequence G description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 6) chain D residue 142 type sequence S description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 7) chain D residue 144 type sequence V description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 8) chain D residue 145 type sequence A description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 9) chain D residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 10) chain D residue 245 type sequence F description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 11) chain D residue 249 type sequence M description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 12) chain D residue 252 type sequence F description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 13) chain D residue 253 type sequence D description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 14) chain D residue 256 type sequence R description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 15) chain D residue 324 type sequence R description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 16) chain D residue 326 type sequence T description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 17) chain D residue 375 type sequence Y description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 18) chain D residue 376 type sequence G description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 19) chain D residue 377 type sequence G description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 20) chain D residue 381 type sequence I description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 21) chain D residue 388 type sequence R description BINDING SITE FOR RESIDUE CO8 D 400 source : AC4 22) chain D residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 23) chain D residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 24) chain D residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 25) chain D residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 26) chain D residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 27) chain D residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 28) chain D residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 29) chain D residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 30) chain D residue 352 type sequence G description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 31) chain D residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 32) chain D residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 33) chain D residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 34) chain D residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 35) chain D residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 36) chain D residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 37) chain D residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 38) chain D residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 39) chain D residue 222 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 40) chain D residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 41) chain D residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 42) chain D residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 43) chain D residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC8 44) chain D residue 376 type ACT_SITE sequence G description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 45) chain D 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 46) chain D 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 47) chain D 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 48) chain D 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 49) chain D 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 50) chain D residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 51) chain D residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 52) chain D residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 53) chain D residue 376 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 54) chain D residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 55) chain D residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 56) chain D residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 57) chain D residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 58) chain D residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 59) chain D residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 60) chain D residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 61) chain D residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 62) chain D residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8

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