eF-site ID 1egc-B PDB Code 1egc Chain B 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 B:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKERPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYGGTSQIQRLIVAREHIDKYKN Description Functional site 1) chain B residue 255 type sequence E description CATALYTIC BASE IN CHAIN B source : CA2 2) chain B residue 284 type sequence F description BINDING SITE FOR RESIDUE CO8 A 400 source : AC1 3) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 4) chain B residue 103 type sequence L description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 5) chain B residue 136 type sequence T description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 6) chain B residue 141 type sequence G description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 7) chain B residue 142 type sequence S description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 8) chain B residue 144 type sequence V description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 9) chain B residue 145 type sequence A description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 10) chain B residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 11) chain B residue 245 type sequence F description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 12) chain B residue 249 type sequence M description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 13) chain B residue 252 type sequence F description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 14) chain B residue 253 type sequence D description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 15) chain B residue 256 type sequence R description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 16) chain B residue 259 type sequence V description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 17) chain B residue 326 type sequence T description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 18) chain B residue 375 type sequence Y description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 19) chain B residue 376 type sequence G description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 20) chain B residue 377 type sequence G description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 21) chain B residue 381 type sequence I description BINDING SITE FOR RESIDUE CO8 B 400 source : AC2 22) chain B residue 191 type sequence N description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 23) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE CO8 C 400 source : AC3 24) chain B residue 277 type sequence Y description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 25) chain B residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 26) chain B residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 27) chain B residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 28) chain B residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 29) chain B residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 30) chain B residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 31) chain B residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 32) chain B residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC5 33) chain B residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 34) chain B residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 35) chain B residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 36) chain B residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 37) chain B residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 38) chain B residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 39) chain B residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 40) chain B residue 222 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 41) chain B residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 42) chain B residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 43) chain B residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 44) chain B residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC6 45) chain B residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC7 46) chain B residue 376 type ACT_SITE sequence G description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 47) chain B 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 48) chain B 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 49) chain B 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 50) chain B 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 51) chain B 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 52) chain B residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 53) chain B residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 54) chain B residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 55) chain B residue 376 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 56) chain B residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 57) chain B residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 59) chain B residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 60) chain B residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 62) chain B residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 63) chain B residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 64) chain B residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8

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