eF-site ID 1a4z-ABCD PDB Code 1a4z Chain A, B, C, D click to enlarge Title ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA COMPLEX WITH NAD (REDUCED) AND SAMARIUM (III) Classification OXIDOREDUCTASE Compound ALDEHYDE DEHYDROGENASE Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDV ICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRL LNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLK CLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIP WNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL IKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGST EVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAV EQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAK SRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKL LCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQI LKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQ AGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTE VKTVTVRVPQKNS B:  VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDV ICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRL LNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLK CLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIP WNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL IKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGST EVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAV EQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAK SRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKL LCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQI LKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQ AGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTE VKTVTVRVPQKNS C:  VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDV ICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRL LNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLK CLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIP WNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL IKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGST EVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAV EQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAK SRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKL LCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQI LKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQ AGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTE VKTVTVRVPQKNS D:  VPTPNQQPEVLYNQIFINNEWHDAVSKKTFPTVNPSTGDV ICHVAEGDKADVDRAVKAARAAFQLGSPWRRMDASERGRL LNRLADLIERDRTYLAALETLDNGKPYIISYLVDLDMVLK CLRYYAGWADKYHGKTIPIDGDYFSYTRHEPVGVCGQIIP WNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANL IKEAGFPPGVVNVIPGFGPTAGAAIASHEDVDKVAFTGST EVGHLIQVAAGKSNLKRVTLEIGGKSPNIIMSDADMDWAV EQAHFALFFNQGQCCCAGSRTFVQEDIYAEFVERSVARAK SRVVGNPFDSRTEQGPQVDETQFKKVLGYIKSGKEEGLKL LCGGGAAADRGYFIQPTVFGDLQDGMTIAKEEIFGPVMQI LKFKSMEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQ AGTVWVNCYDVFGAQSPFGGYKLSGSGRELGEYGLQAYTE VKTVTVRVPQKNS Description Functional site 1) chain A residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 2) chain A residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 3) chain A residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 4) chain A residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 5) chain A residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 6) chain A residue 174 type sequence M description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 7) chain A residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 8) chain A residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 9) chain A residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 10) chain A residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 11) chain A residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 12) chain A residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 13) chain A residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 14) chain A residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 15) chain A residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 16) chain A residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 17) chain A residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 18) chain A residue 252 type sequence L description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 19) chain A residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 20) chain A residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 21) chain A residue 269 type sequence I description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 22) chain A residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 23) chain A residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 24) chain A residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 25) chain A residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD A 501 source : AC5 26) chain B residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 27) chain B residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 28) chain B residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 29) chain B residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 30) chain B residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 31) chain B residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 32) chain B residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 33) chain B residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 34) chain B residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 35) chain B residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 36) chain B residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 37) chain B residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 38) chain B residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 39) chain B residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 40) chain B residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 41) chain B residue 252 type sequence L description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 42) chain B residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 43) chain B residue 269 type sequence I description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 44) chain B residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 45) chain B residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 46) chain B residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 47) chain B residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD B 501 source : AC6 48) chain C residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 49) chain C residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 50) chain C residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 51) chain C residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 52) chain C residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 53) chain C residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 54) chain C residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 55) chain C residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 56) chain C residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 57) chain C residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 58) chain C residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 59) chain C residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 60) chain C residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 61) chain C residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 62) chain C residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 63) chain C residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 64) chain C residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 65) chain C residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 66) chain C residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 67) chain C residue 269 type sequence I description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 68) chain C residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 69) chain C residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 70) chain C residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 71) chain C residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD C 501 source : AC7 72) chain D residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 73) chain D residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 74) chain D residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 75) chain D residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 76) chain D residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 77) chain D residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 78) chain D residue 194 type sequence A description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 79) chain D residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 80) chain D residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 81) chain D residue 226 type sequence P description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 82) chain D residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 83) chain D residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 84) chain D residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 85) chain D residue 244 type sequence T description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 86) chain D residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 87) chain D residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 88) chain D residue 249 type sequence V description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 89) chain D residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 90) chain D residue 268 type sequence E description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 91) chain D residue 269 type sequence I description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 92) chain D residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 93) chain D residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 94) chain D residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 95) chain D residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD D 501 source : AC8 96) chain A residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI1 97) chain B residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI1 98) chain C residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI1 99) chain D residue 268 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI1 100) chain A residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI2 101) chain B residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI2 102) chain C residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI2 103) chain D residue 302 type ACT_SITE sequence C description Nucleophile => ECO:0000305|PubMed:9195888 source Swiss-Prot : SWS_FT_FI2 104) chain A residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 105) chain B residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 106) chain B residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 107) chain B residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 108) chain C residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 109) chain C residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 110) chain C residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 111) chain C residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 112) chain C residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 113) chain C residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 114) chain D residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 115) chain A residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 116) chain D residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 117) chain D residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 118) chain D residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 119) chain D residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 120) chain D residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 121) chain A residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 122) chain A residue 245 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 123) chain A residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 124) chain A residue 399 type BINDING sequence E description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 125) chain B residue 166 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 126) chain B residue 192 type BINDING sequence K description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 127) chain B residue 225 type BINDING sequence G description BINDING => ECO:0000269|PubMed:9195888, ECO:0007744|PDB:1A4Z source Swiss-Prot : SWS_FT_FI3 128) chain A residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:9195888 source Swiss-Prot : SWS_FT_FI4 129) chain B residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:9195888 source Swiss-Prot : SWS_FT_FI4 130) chain C residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:9195888 source Swiss-Prot : SWS_FT_FI4 131) chain D residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000269|PubMed:9195888 source Swiss-Prot : SWS_FT_FI4 132) chain A residue 295-306 type prosite sequence FFNQGQCCCAGS description ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNQGQCCCAGS source prosite : PS00070 133) chain A residue 267-274 type prosite sequence LEIGGKSP description ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LEIGGKSP source prosite : PS00687 134) chain A residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 135) chain A residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 136) chain B residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 137) chain B residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 138) chain B residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 139) chain B residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 140) chain B residue 358 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 141) chain B residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 142) chain B residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 143) chain B residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 144) chain B residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 145) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 146) chain B residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 147) chain C residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 148) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 149) chain C residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 150) chain C residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 151) chain C residue 358 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 152) chain C residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 153) chain C residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 154) chain C residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 155) chain C residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 156) chain A residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 157) chain C residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 158) chain D residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 159) chain D residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 160) chain D residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 161) chain D residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 162) chain D residue 358 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 163) chain D residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 164) chain D residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 165) chain D residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 166) chain D residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 167) chain A residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 168) chain D residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 169) chain A residue 358 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 170) chain A residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 171) chain A residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 172) chain A residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 173) chain A residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5

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