eF-site ID 1ege-ABCD PDB Code 1ege Chain A, B, C, D 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 A:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYEGTSQIQRLIVAREHIDKYKN B:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYEGTSQIQRLIVAREHIDKYKN C:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYEGTSQIQRLIVAREHIDKYKN D:  LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP VPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAY GCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPL MCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITN GGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIG RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM GAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLV EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYA SIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDA KIYQIYEGTSQIQRLIVAREHIDKYKN Description Functional site 1) chain A residue 376 type sequence E description CATALYTIC BASE IN CHAIN A source : CA1 2) chain B residue 376 type sequence E description CATALYTIC BASE IN CHAIN B source : CA2 3) chain C residue 376 type sequence E description CATALYTIC BASE IN CHAIN C source : CA3 4) chain D residue 376 type sequence E description CATALYTIC BASE IN CHAIN D source : CA4 5) chain A residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 6) chain A residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 7) chain A residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 8) chain A residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 9) chain A residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 10) chain A residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 11) chain A residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 12) chain A residue 214 type sequence N description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 13) chain A residue 222 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 14) chain A residue 371 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 15) chain A residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 16) chain A residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 17) chain A residue 381 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 18) chain B residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 19) chain B residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 20) chain B residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 21) chain B residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 22) chain B residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 23) chain B residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 24) chain B residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 25) chain B residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 26) chain B residue 352 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 27) chain B residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 28) chain D residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD A 399 source : AC1 29) chain A residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 30) chain A residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 31) chain A residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 32) chain A residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 33) chain A residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 34) chain A residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 35) chain A residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 36) chain A residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 37) chain B residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 38) chain B residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 39) chain B residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 40) chain B residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 41) chain B residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 42) chain B residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 43) chain B residue 167 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 44) chain B residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 45) chain B residue 214 type sequence N description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 46) chain B residue 371 type sequence I description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 47) chain B residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 48) chain B residue 376 type sequence E description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 49) chain B residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 50) chain B residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 51) chain C residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD B 399 source : AC2 52) chain B residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 53) chain C residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 54) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 55) chain C residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 56) chain C residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 57) chain C residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 58) chain C residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 59) chain C residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 60) chain C residue 222 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 61) chain C residue 371 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 62) chain C residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 63) chain C residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 64) chain C residue 376 type sequence E description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 65) chain C residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 66) chain C residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 67) chain D residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 68) chain D residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 69) chain D residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 70) chain D residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 71) chain D residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 72) chain D residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 73) chain D residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 74) chain D residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 75) chain D residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD C 399 source : AC3 76) chain A residue 292 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 77) chain C residue 281 type sequence R description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 78) chain C residue 283 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 79) chain C residue 284 type sequence F description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 80) chain C residue 288 type sequence L description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 81) chain C residue 291 type sequence H description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 82) chain C residue 294 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 83) chain C residue 349 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 84) chain C residue 350 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 85) chain C residue 352 type sequence G description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 86) chain C residue 353 type sequence G description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 87) chain D residue 133 type sequence Y description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 88) chain D residue 135 type sequence V description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 89) chain D residue 136 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 90) chain D residue 141 type sequence G description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 91) chain D residue 142 type sequence S description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 92) chain D residue 166 type sequence W description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 93) chain D residue 168 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 94) chain D residue 214 type sequence N description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 95) chain D residue 222 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 96) chain D residue 371 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 97) chain D residue 374 type sequence I description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 98) chain D residue 375 type sequence Y description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 99) chain D residue 376 type sequence E description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 100) chain D residue 378 type sequence T description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 101) chain D residue 380 type sequence Q description BINDING SITE FOR RESIDUE FAD D 399 source : AC4 102) chain A residue 376 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 103) 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 104) chain C residue 376 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 105) chain D residue 376 type ACT_SITE sequence E description Proton acceptor => ECO:0000269|PubMed:1970566, ECO:0000269|PubMed:8823176 source Swiss-Prot : SWS_FT_FI1 106) chain D residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 107) chain D residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 108) chain D residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 109) chain D residue 376 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 110) chain B residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 111) chain B residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 112) chain A residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 113) chain A residue 376 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 114) chain C residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 115) chain C residue 256 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 116) chain C residue 376 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 117) chain B residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 118) chain B residue 376 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 119) chain C residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 120) chain A residue 142 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 121) chain A residue 253 type BINDING sequence D description BINDING => ECO:0000269|PubMed:8823176, ECO:0007744|PDB:1EGC source Swiss-Prot : SWS_FT_FI3 122) chain B residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 123) chain B residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 124) chain C residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 125) chain C residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 126) chain C residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 127) chain C residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 128) chain C residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 129) chain D residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 130) chain D residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 131) chain D residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 132) chain D residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 133) chain D residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 134) chain A residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 135) chain A residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 136) chain A residue 234 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 137) chain A residue 246 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 138) chain B residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 139) chain B residue 187 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 140) chain B residue 192 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 141) chain A residue 44 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI5 142) chain A residue 134-146 type prosite sequence CVTEPGAGSDVAG description ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CVTEpgAGSDvaG source prosite : PS00072 143) chain A residue 349-368 type prosite sequence QILGGNGFNTEYPVEKLMRD description ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiLGGnGFntEypveKlmrD source prosite : PS00073 144) 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 145) 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 146) 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 147) 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 148) 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 149) 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 150) 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 151) 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 152) 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 153) 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 154) 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 155) 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 156) 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 157) 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 158) 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 159) 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 160) 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 161) 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 162) 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 163) 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 164) chain C residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 165) chain D residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 166) chain A residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 167) chain B residue 154 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI6 168) chain C residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 169) chain C residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 170) chain D residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 171) chain D residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 172) chain A residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 173) chain A residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 174) chain B residue 254 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 175) chain B residue 276 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 176) chain C residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8 177) chain D residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8 178) chain A residue 326 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P45952 source Swiss-Prot : SWS_FT_FI8 179) 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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