eF-site ID 1ege-B PDB Code 1ege Chain B 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 ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence B:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYEGTSQIQRLIVAREHIDKYKN Description Functional site 1) chain B residue 376 type sequence E description CATALYTIC BASE IN CHAIN B source : CA2 2) chain B residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 3) chain B residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 4) chain B residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 5) chain B residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 6) chain B residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 7) chain B residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 8) chain B residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 9) chain B residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 10) chain B residue 352 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 11) chain B residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 12) chain B residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 13) chain B residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 14) chain B residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 15) chain B residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 16) chain B residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 17) chain B residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 18) chain B residue 167 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 19) chain B residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 20) chain B residue 214 type sequence N description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 21) chain B residue 371 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 22) chain B residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 23) chain B residue 376 type sequence E description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 24) chain B residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 25) chain B residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 26) chain B residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 27) chain B residue 376 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 28) 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 29) 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 30) 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 31) chain B residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 32) chain B residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 33) chain B residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 34) chain B residue 376 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 35) 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 36) 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 37) chain B residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 39) chain B residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 40) chain B residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 41) chain B residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 42) chain B residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 43) chain B residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 44) chain B residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 45) 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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