eF-site ID 1kyo-ABCDEFGHIJKLMNOPQRSTUVW PDB Code 1kyo 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 YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C Classification OXIDOREDUCTASE/ELECTRON TRANSPORT Compound UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  AEVTQLSNGIVVATEHNPAHTASVGVVFGSGAANENPYNN GVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVS SLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQ VQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLEN LVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKN LSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEG EPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQ EYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHFT LKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDA NLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLW DQDIAIAGTGQIEGLLDYMRIRSDMSMMRW B:  LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNF QNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKD DLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFA DKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLV SKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAV VSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPI ELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL C:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK D:  MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVC AACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQ GNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGG SIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEP EHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV FNPPK E:  KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR IRKGPAPLNLEIPAYEFDGDKVIVG F:  DTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPG YADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK G:  QSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLG LKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTE LTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDN IEVSK H:  GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIF HNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLY SKAGREELERVNV I:  SSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENH NKGKLWKDVKAKI J:  EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRL FPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFF LKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV SSAWRHP K:  DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKP DGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEP EDIATYFCQHHIKFPWTFGAGTKLEIK L:  AEVTQLSNGIVVATEHNPAHTASVGVVFGSGAANENPYNN GVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVS SLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQ VQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLEN LVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKN LSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEG EPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQ EYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHFT LKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDA NLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLW DQDIAIAGTGQIEGLLDYMRIRSDMSMMRW M:  LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNF QNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKD DLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFA DKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLV SKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAV VSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPI ELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL N:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK O:  MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVC AACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQ GNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGG SIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEP EHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV FNPPK P:  KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR IRKGPAPLNLEIPAYEFDGDKVIVG Q:  DTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPG YADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK R:  QSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLG LKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTE LTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDN IEVSK S:  GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIF HNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLY SKAGREELERVNV T:  SSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENH NKGKLWKDVKAKI U:  EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRL FPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFF LKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV SSAWRHP V:  DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKP DGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEP EDIATYFCQHHIKFPWTFGAGTKLEIK W:  TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGI FGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPXKYI PGTKMAFGGLKKEKDRNDLITYLKKACE Description Functional site 1) chain C residue 43 type sequence Q description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 2) chain C residue 47 type sequence G description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 3) chain C residue 48 type sequence I description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 4) chain C residue 50 type sequence M description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 5) chain C residue 51 type sequence A description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 6) chain C residue 79 type sequence R description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 7) chain C residue 82 type sequence H description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 8) chain C residue 83 type sequence A description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 9) chain C residue 127 type sequence T description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 10) chain C residue 128 type sequence A description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 11) chain C residue 131 type sequence G description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 12) chain C residue 132 type sequence Y description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 13) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 14) chain C residue 183 type sequence H description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 15) chain C residue 184 type sequence Y description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 16) chain C residue 187 type sequence P description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 17) chain C residue 30 type sequence W description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 18) chain C residue 33 type sequence G description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 19) chain C residue 96 type sequence H description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 20) chain C residue 97 type sequence M description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 21) chain C residue 99 type sequence K description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 22) chain C residue 105 type sequence S description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 23) chain C residue 113 type sequence L description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 24) chain C residue 117 type sequence G description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 25) chain C residue 118 type sequence V description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 26) chain C residue 120 type sequence I description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 27) chain C residue 197 type sequence H description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 28) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 29) chain C residue 206 type sequence S description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 30) chain C residue 207 type sequence S description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 31) chain D residue 100 type sequence V description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 32) chain D residue 101 type sequence C description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 33) chain D residue 104 type sequence C description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 34) chain D residue 105 type sequence H description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 35) chain D residue 169 type sequence N description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 36) chain D residue 180 type sequence I description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 37) chain D residue 184 type sequence R description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 38) chain D residue 190 type sequence Y description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 39) chain D residue 218 type sequence F description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 40) chain D residue 224 type sequence A description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 41) chain D residue 225 type sequence M description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 42) chain D residue 228 type sequence V description BINDING SITE FOR RESIDUE HEC D 503 source : AC3 43) chain E residue 159 type sequence C description BINDING SITE FOR RESIDUE FES E 504 source : AC4 44) chain E residue 161 type sequence H description BINDING SITE FOR RESIDUE FES E 504 source : AC4 45) chain E residue 162 type sequence L description BINDING SITE FOR RESIDUE FES E 504 source : AC4 46) chain E residue 178 type sequence C description BINDING SITE FOR RESIDUE FES E 504 source : AC4 47) chain E residue 181 type sequence H description BINDING SITE FOR RESIDUE FES E 504 source : AC4 48) chain E residue 183 type sequence S description BINDING SITE FOR RESIDUE FES E 504 source : AC4 49) chain C residue 125 type sequence I description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 50) chain C residue 126 type sequence A description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 51) chain C residue 143 type sequence G description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 52) chain C residue 146 type sequence V description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 53) chain C residue 147 type sequence I description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 54) chain C residue 165 type sequence L description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 55) chain C residue 270 type sequence V description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 56) chain C residue 271 type sequence P description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 57) chain C residue 272 type sequence E description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 58) chain C residue 278 type sequence F description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 59) chain C residue 279 type sequence Y description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 60) chain C residue 295 type sequence M description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 61) chain P residue 181 type sequence H description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 62) chain N residue 43 type sequence Q description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 63) chain N residue 47 type sequence G description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 64) chain N residue 48 type sequence I description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 65) chain N residue 50 type sequence M description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 66) chain N residue 79 type sequence R description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 67) chain N residue 82 type sequence H description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 68) chain N residue 83 type sequence A description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 69) chain N residue 89 type sequence F description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 70) chain N residue 128 type sequence A description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 71) chain N residue 131 type sequence G description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 72) chain N residue 132 type sequence Y description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 73) chain N residue 135 type sequence V description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 74) chain N residue 183 type sequence H description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 75) chain N residue 184 type sequence Y description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 76) chain N residue 187 type sequence P description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 77) chain N residue 30 type sequence W description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 78) chain N residue 33 type sequence G description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 79) chain N residue 36 type sequence L description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 80) chain N residue 96 type sequence H description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 81) chain N residue 99 type sequence K description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 82) chain N residue 105 type sequence S description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 83) chain N residue 113 type sequence L description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 84) chain N residue 114 type sequence W description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 85) chain N residue 117 type sequence G description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 86) chain N residue 194 type sequence V description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 87) chain N residue 197 type sequence H description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 88) chain N residue 201 type sequence L description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 89) chain N residue 206 type sequence S description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 90) chain N residue 207 type sequence S description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 91) chain O residue 100 type sequence V description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 92) chain O residue 101 type sequence C description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 93) chain O residue 104 type sequence C description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 94) chain O residue 105 type sequence H description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 95) chain O residue 169 type sequence N description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 96) chain O residue 175 type sequence P description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 97) chain O residue 184 type sequence R description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 98) chain O residue 190 type sequence Y description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 99) chain O residue 191 type sequence I description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 100) chain O residue 218 type sequence F description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 101) chain O residue 224 type sequence A description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 102) chain O residue 225 type sequence M description BINDING SITE FOR RESIDUE HEC O 523 source : AC8 103) chain P residue 159 type sequence C description BINDING SITE FOR RESIDUE FES P 524 source : AC9 104) chain P residue 161 type sequence H description BINDING SITE FOR RESIDUE FES P 524 source : AC9 105) chain P residue 162 type sequence L description BINDING SITE FOR RESIDUE FES P 524 source : AC9 106) chain P residue 178 type sequence C description BINDING SITE FOR RESIDUE FES P 524 source : AC9 107) chain P residue 180 type sequence C description BINDING SITE FOR RESIDUE FES P 524 source : AC9 108) chain P residue 181 type sequence H description BINDING SITE FOR RESIDUE FES P 524 source : AC9 109) chain P residue 183 type sequence S description BINDING SITE FOR RESIDUE FES P 524 source : AC9 110) chain E residue 181 type sequence H description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 111) chain N residue 122 type sequence T description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 112) chain N residue 125 type sequence I description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 113) chain N residue 126 type sequence A description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 114) chain N residue 129 type sequence F description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 115) chain N residue 130 type sequence L description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 116) chain N residue 139 type sequence M description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 117) chain N residue 146 type sequence V description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 118) chain N residue 147 type sequence I description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 119) chain N residue 269 type sequence I description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 120) chain N residue 271 type sequence P description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 121) chain N residue 272 type sequence E description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 122) chain N residue 279 type sequence Y description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 123) chain N residue 295 type sequence M description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 124) chain N residue 296 type sequence F description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 125) chain W residue 18 type sequence R description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 126) chain W residue 19 type sequence C description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 127) chain W residue 22 type sequence C description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 128) chain W residue 23 type sequence H description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 129) chain W residue 33 type sequence V description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 130) chain W residue 34 type sequence G description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 131) chain W residue 40 type sequence I description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 132) chain W residue 45 type sequence S description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 133) chain W residue 46 type sequence G description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 134) chain W residue 51 type sequence Y description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 135) chain W residue 53 type sequence Y description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 136) chain W residue 54 type sequence T description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 137) chain W residue 57 type sequence N description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 138) chain W residue 64 type sequence W description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 139) chain W residue 72 type sequence Y description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 140) chain W residue 83 type sequence T description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 141) chain W residue 84 type sequence K description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 142) chain W residue 85 type sequence M description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 143) chain W residue 87 type sequence F description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 144) chain E residue 181 type catalytic sequence H description 208 source MCSA : MCSA1 145) chain C residue 206 type catalytic sequence S description 208 source MCSA : MCSA1 146) chain C residue 228 type catalytic sequence K description 208 source MCSA : MCSA1 147) chain C residue 229 type catalytic sequence D description 208 source MCSA : MCSA1 148) chain C residue 272 type catalytic sequence E description 208 source MCSA : MCSA1 149) chain P residue 181 type catalytic sequence H description 208 source MCSA : MCSA2 150) chain N residue 206 type catalytic sequence S description 208 source MCSA : MCSA2 151) chain N residue 228 type catalytic sequence K description 208 source MCSA : MCSA2 152) chain N residue 229 type catalytic sequence D description 208 source MCSA : MCSA2 153) chain N residue 272 type catalytic sequence E description 208 source MCSA : MCSA2 154) chain W residue 20 type BINDING sequence L description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 155) 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 156) chain W residue 23 type BINDING sequence H description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 157) 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 158) 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 159) 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 160) 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 161) 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 162) 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 163) 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 164) chain W residue 24 type BINDING sequence T 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 165) 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 166) chain N residue 111-135 type BINDING sequence VTLWNVGVIIFTLTIATAFLGYCCV 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 167) 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 168) 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 169) 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 170) 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 171) 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 172) chain W residue 86 type BINDING sequence A 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 173) chain C residue 111-135 type BINDING sequence VTLWNVGVIIFTLTIATAFLGYCCV 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 174) 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 175) 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 176) 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 177) 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 178) 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 179) 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 180) chain W residue 78 type MOD_RES sequence K 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 181) chain S residue 81-94 type MOD_RES sequence YSKAGREELERVNV 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 182) 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 183) 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 184) 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 185) 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 186) 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 187) 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 188) 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 189) 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 190) chain B residue 37-59 type prosite sequence GGSRYATKDGVAHLLNRFNFQNT description INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT source prosite : PS00143 191) chain W residue 79 type MOD_RES sequence Y description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4 192) 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 193) 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 194) 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 195) 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 196) 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 197) 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 198) 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 199) 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 200) 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 201) 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 202) 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 203) 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 204) 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 205) 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 206) 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

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