eF-site ID 3cx5-ABCDEFGHIJKLMNOPQRSTUVW PDB Code 3cx5 Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W Title Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. Classification OXIDOREDUCTASE Compound Cytochrome b-c1 complex subunit 1, mitochondrial Source ORGANISM_COMMON: yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  AEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYN NGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIV SSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLK QVQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLE NLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESK NLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVE GEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNI QEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHF TLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVND ANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRL WDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW B:  LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNF QNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKD DLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFA DKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLV SKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAV VSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPI ELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL C:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK D:  MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVC AACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQ GNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGG SIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEP EHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV FNPPKPRK E:  KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR IRKGPAPLNLEIPAYEFDGDKVIVG F:  VTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPG YADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK G:  PQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKL GLKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQT ELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELD NIEVSK H:  GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIF HNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLY SKAGREELERVNV I:  SFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYE NHNKGKLWKDVKARIAA J:  EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRL FPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFF LKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV SSAWRHP K:  DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKP DGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEP EDIATYFCQHHIKFPWTFGAGTKLEIK L:  AEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYN NGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIV SSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLK QVQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLE NLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESK NLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVE GEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNI QEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHF TLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVND ANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRL WDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW M:  LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNF QNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKD DLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFA DKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLV SKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAV VSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPI ELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL N:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK O:  MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVC AACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQ GNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGG SIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEP EHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV FNPPKPRK P:  KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR IRKGPAPLNLEIPAYEFDGDKVIVG Q:  VTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPG YADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK R:  PQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKL GLKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQT ELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELD NIEVSK S:  GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIF HNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLY SKAGREELERVNV T:  SFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYE NHNKGKLWKDVKARIAA U:  EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRL FPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFF LKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV SSAWRHP V:  DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKP DGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEP EDIATYFCQHHIKFPWTFGAGTKLEIK W:  TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGI FGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPXKYI PGTKMAFGGLKKEKDRNDLITYLKKACE Description Functional site 1) chain E residue 178 type MOD_RES sequence C description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 2) chain E residue 181 type MOD_RES sequence H description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 3) chain P residue 159 type MOD_RES sequence C description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 4) chain P residue 161 type MOD_RES sequence H description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 5) chain P residue 178 type MOD_RES sequence C description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 6) chain P residue 181 type MOD_RES sequence H description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 7) chain W residue 78 type MOD_RES sequence K description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 8) chain E residue 161 type MOD_RES sequence H description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 9) chain C residue 183 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI5 10) chain C residue 197 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI5 11) chain N residue 82 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI5 12) chain N residue 96 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI5 13) chain N residue 183 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI5 14) chain N residue 197 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI5 15) chain D residue 105 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI5 16) chain O residue 105 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI5 17) chain B residue 37-59 type prosite sequence GGSRYATKDGVAHLLNRFNFQNT description INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT source prosite : PS00143 18) chain E residue 181 type catalytic sequence H description 208 source MCSA : MCSA1 19) chain C residue 206 type catalytic sequence S description 208 source MCSA : MCSA1 20) chain C residue 228 type catalytic sequence K description 208 source MCSA : MCSA1 21) chain C residue 229 type catalytic sequence D description 208 source MCSA : MCSA1 22) chain C residue 272 type catalytic sequence E description 208 source MCSA : MCSA1 23) chain P residue 181 type catalytic sequence H description 208 source MCSA : MCSA2 24) chain N residue 206 type catalytic sequence S description 208 source MCSA : MCSA2 25) chain N residue 228 type catalytic sequence K description 208 source MCSA : MCSA2 26) chain N residue 229 type catalytic sequence D description 208 source MCSA : MCSA2 27) chain N residue 272 type catalytic sequence E description 208 source MCSA : MCSA2 28) chain W residue 22 type BINDING sequence C description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 29) chain C residue 205-223 type BINDING sequence GSSNPLGITGNLDRIPMHS description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 30) chain C residue 309-319 type BINDING sequence DRSVVRGNTFK description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 365-385 type BINDING sequence IIVPVISTIENVLFYIGRVNK description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 32) chain N residue 1-27 type BINDING sequence MAFRKSNVYLSLVNSYIIDSPQPSSIN description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 33) chain N residue 103-110 type BINDING sequence YGSYRSPR description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 34) chain N residue 205-223 type BINDING sequence GSSNPLGITGNLDRIPMHS description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 35) chain N residue 309-319 type BINDING sequence DRSVVRGNTFK description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 36) chain N residue 365-385 type BINDING sequence IIVPVISTIENVLFYIGRVNK description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 37) chain W residue 19 type BINDING sequence C description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 38) chain W residue 85 type BINDING sequence M description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 39) chain C residue 111-135 type BINDING sequence VTLWNVGVIIFILTIATAFLGYCCV description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 40) chain C residue 173-204 type BINDING sequence NPTIQRFFALHYLVPFIIAAMVIMHLMALHIH description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 41) chain C residue 224-246 type BINDING sequence YFIFKDLVTVFLFMLILALFVFY description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 42) chain C residue 288-308 type BINDING sequence KLLGVITMFAAILVLLVLPFT description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 43) chain C residue 320-340 type BINDING sequence VLSKFFFFIFVFNFVLLGQIG description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 44) chain C residue 348-364 type BINDING sequence YVLMGQIATFIYFAYFL description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 45) chain N residue 28-51 type BINDING sequence YWWNMGSLLGLCLVIQIVTGIFMA description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 46) chain N residue 75-102 type BINDING sequence GYILRYLHANGASFFFMVMFMHMAKGLY description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 47) chain N residue 111-135 type BINDING sequence VTLWNVGVIIFILTIATAFLGYCCV description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 48) chain N residue 173-204 type BINDING sequence NPTIQRFFALHYLVPFIIAAMVIMHLMALHIH description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 49) chain N residue 224-246 type BINDING sequence YFIFKDLVTVFLFMLILALFVFY description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 50) chain N residue 288-308 type BINDING sequence KLLGVITMFAAILVLLVLPFT description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 51) chain N residue 320-340 type BINDING sequence VLSKFFFFIFVFNFVLLGQIG description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 52) chain N residue 348-364 type BINDING sequence YVLMGQIATFIYFAYFL description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 53) chain W residue 23 type BINDING sequence H description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 54) chain C residue 247-287 type MOD_RES sequence SPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIP D description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 55) chain C residue 341-347 type MOD_RES sequence ACHVEVP description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 56) chain N residue 52-74 type MOD_RES sequence MHYSSNIELAFSSVEHIMRDVHN description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 57) chain N residue 136-172 type MOD_RES sequence YGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVS description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 58) chain N residue 247-287 type MOD_RES sequence SPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIP D description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 59) chain N residue 341-347 type MOD_RES sequence ACHVEVP description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 60) chain W residue 77 type MOD_RES sequence X description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 61) chain D residue 225 type BINDING sequence M description axial binding residue => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI6 62) chain O residue 225 type BINDING sequence M description axial binding residue => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI6

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