eF-site ID 2ibz-ABCDEFGHIXY PDB Code 2ibz Chain A, B, C, D, E, F, G, H, I, X, Y click to enlarge Title Yeast Cytochrome BC1 Complex with Stigmatellin Classification OXIDOREDUCTASE Compound Ubiquinol-cytochrome-c reductase complex core protein 1 Source ORGANISM_COMMON: baker's 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 FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK D:  MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVC AACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQ GNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGG SIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEP EHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV FNPPK E:  KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR IRKGPAPLNLEIPAYEFDGDKVIVG F:  QSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLG LKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTE LTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDN IEVSK G:  GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIF HNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLY SKAGREELERVNV H:  VTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPG YADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK I:  SSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENH NKGKLWKDVKARIAA X:  EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRL FPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFF LKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV SSAWRHP Y:  DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKP DGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEP EDIATYFCQHHIKFPWTFGAGTKLEIK Description (1)  Ubiquinol-cytochrome-c reductase complex core protein 1, mitochondrial precursor (E.C.1.10.2.2 ), Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor (E.C.1.10.2.2 ), Cytochrome b (E.C.1.10.2.2 ), Cytochrome c1, heme protein, mitochondrial precursor (E.C.1.10.2.2 ), Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (E.C.1.10.2.2), Ubiquinol-cytochrome c reductase complex 17 kDa protein (E.C.1.10.2.2 ), Ubiquinol-cytochrome c reductase complex 14 kDa protein (E.C.1.10.2.2 ), Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C (E.C.1.10.2.2 ), Ubiquinol-cytochrome c reductase complex 7.3 kDa protein (E.C.1.10.2.2 ), VH chain of antibody fragment, VL chain of antibody fragment Functional site 1) chain C residue 40 type sequence L description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 2) chain C residue 43 type sequence Q description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 3) chain C residue 47 type sequence G description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 4) chain C residue 48 type sequence I description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 5) chain C residue 50 type sequence M description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 6) chain C residue 51 type sequence A description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 7) chain C residue 79 type sequence R description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 8) chain C residue 82 type sequence H description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 9) chain C residue 89 type sequence F description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 10) chain C residue 127 type sequence T description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 11) chain C residue 128 type sequence A description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 12) chain C residue 131 type sequence G description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 13) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 14) chain C residue 183 type sequence H description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 15) chain C residue 184 type sequence Y description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 16) chain C residue 187 type sequence P description BINDING SITE FOR RESIDUE HEC C 401 source : AC1 17) chain C residue 30 type sequence W description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 18) chain C residue 33 type sequence G description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 19) chain C residue 36 type sequence L description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 20) chain C residue 96 type sequence H description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 21) chain C residue 99 type sequence K description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 22) chain C residue 105 type sequence S description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 23) chain C residue 113 type sequence L description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 24) chain C residue 114 type sequence W description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 25) chain C residue 117 type sequence G description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 26) chain C residue 118 type sequence V description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 27) chain C residue 120 type sequence I description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 28) chain C residue 197 type sequence H description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 29) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 30) chain C residue 206 type sequence S description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 31) chain C residue 207 type sequence S description BINDING SITE FOR RESIDUE HEC C 402 source : AC2 32) chain D residue 100 type sequence V description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 33) chain D residue 101 type sequence C description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 34) chain D residue 104 type sequence C description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 35) chain D residue 105 type sequence H description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 36) chain D residue 169 type sequence N description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 37) chain D residue 175 type sequence P description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 38) chain D residue 184 type sequence R description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 39) chain D residue 190 type sequence Y description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 40) chain D residue 191 type sequence I description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 41) chain D residue 218 type sequence F description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 42) chain D residue 223 type sequence I description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 43) chain D residue 224 type sequence A description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 44) chain D residue 225 type sequence M description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 45) chain D residue 228 type sequence V description BINDING SITE FOR RESIDUE HEC D 3 source : AC3 46) chain E residue 159 type sequence C description BINDING SITE FOR RESIDUE FES E 4 source : AC4 47) chain E residue 161 type sequence H description BINDING SITE FOR RESIDUE FES E 4 source : AC4 48) chain E residue 162 type sequence L description BINDING SITE FOR RESIDUE FES E 4 source : AC4 49) chain E residue 178 type sequence C description BINDING SITE FOR RESIDUE FES E 4 source : AC4 50) chain E residue 181 type sequence H description BINDING SITE FOR RESIDUE FES E 4 source : AC4 51) chain E residue 183 type sequence S description BINDING SITE FOR RESIDUE FES E 4 source : AC4 52) chain C residue 16 type sequence Y description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC5 53) chain C residue 22 type sequence Q description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC5 54) chain C residue 44 type sequence I description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC5 55) chain C residue 185 type sequence L description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC5 56) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC5 57) chain C residue 206 type sequence S description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC5 58) chain C residue 221 type sequence M description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC5 59) chain C residue 229 type sequence D description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC5 60) chain C residue 125 type sequence I description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 61) chain C residue 146 type sequence V description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 62) chain C residue 271 type sequence P description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 63) chain C residue 272 type sequence E description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 64) chain C residue 275 type sequence L description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 65) chain C residue 279 type sequence Y description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 66) chain C residue 295 type sequence M description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 67) chain C residue 296 type sequence F description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 68) chain E residue 181 type sequence H description BINDING SITE FOR RESIDUE SMA C 505 source : AC6 69) chain E residue 178 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4 source Swiss-Prot : SWS_FT_FI4 70) chain E residue 181 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4 source Swiss-Prot : SWS_FT_FI4 71) chain E residue 159 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4 source Swiss-Prot : SWS_FT_FI4 72) chain E residue 161 type BINDING sequence H description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4 source Swiss-Prot : SWS_FT_FI4 73) 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 74) 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 75) 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 76) chain C 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 77) chain B residue 37-59 type prosite sequence GGSRYATKDGVAHLLNRFNFQNT description INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT source prosite : PS00143 78) chain E residue 181 type catalytic sequence H description 208 source MCSA : MCSA1 79) chain C residue 206 type catalytic sequence S description 208 source MCSA : MCSA1 80) chain C residue 228 type catalytic sequence K description 208 source MCSA : MCSA1 81) chain C residue 229 type catalytic sequence D description 208 source MCSA : MCSA1 82) chain C residue 272 type catalytic sequence E description 208 source MCSA : MCSA1 83) chain C residue 75-102 type TRANSMEM sequence GYILRYLHANGASFFFMVMFMHMAKGLY description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 84) chain C residue 111-135 type TRANSMEM sequence VTLWNVGVIIFTLTIATAFLGYCCV description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 85) chain C residue 173-204 type TRANSMEM sequence NPTIQRFFALHYLVPFIIAAMVIMHLMALHIH description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 86) chain C residue 224-246 type TRANSMEM sequence YFIFKDLVTVFLFMLILALFVFY description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 87) chain C residue 288-308 type TRANSMEM sequence KLLGVITMFAAILVLLVLPFT description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 88) chain C residue 320-340 type TRANSMEM sequence VLSKFFFFIFVFNFVLLGQIG description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 89) chain C residue 348-364 type TRANSMEM sequence YVLMGQIATFIYFAYFL description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 90) chain I residue 19-44 type TRANSMEM sequence GTIFAGAFVFQTVFDTAITSWYENHN description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 91) chain C residue 103-110 type TOPO_DOM sequence YGSYRSPR description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 92) chain C residue 205-223 type TOPO_DOM sequence GSSNPLGITGNLDRIPMHS description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 93) chain C residue 309-319 type TOPO_DOM sequence DRSVVRGNTFK description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 94) chain C residue 365-385 type TOPO_DOM sequence IIVPVISTIENVLFYIGRVNK description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 95) chain C residue 136-172 type TOPO_DOM sequence YGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVS description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI3 96) chain C residue 247-287 type TOPO_DOM sequence SPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIP D description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI3 97) chain C residue 341-347 type TOPO_DOM sequence ACHVEVP description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI3 98) chain G residue 81-94 type TOPO_DOM sequence YSKAGREELERVNV description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI3 99) 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

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