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

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