eF-site ID 1p84-ABCDEFGHIJK PDB Code 1p84 Chain A, B, C, D, E, F, G, H, I, J, K click to enlarge Title HDBT inhibited Yeast Cytochrome bc1 Complex Classification OXIDOREDUCTASE Compound Ubiquinol-cytochrome C reductase complex core protein I 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 FNPPKP E:  KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR IRKGPAPLNLEIPAYEFDGDKVIVG F:  VTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPG YADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK G:  QSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLG LKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTE LTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDN IEVSK H:  GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIF HNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLY SKAGREELERVNV I:  SSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENH NKGKLWKDVKARIAA J:  EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRL FPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFF LKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV SSAWRHP K:  DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKP DGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEP EDIATYFCQHHIKFPWTFGAGTKLEIK Description Functional site 1) chain C residue 40 type sequence L description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 2) chain C residue 43 type sequence Q description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 3) chain C residue 47 type sequence G description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 4) chain C residue 50 type sequence M description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 5) chain C residue 79 type sequence R description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 6) chain C residue 82 type sequence H description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 7) chain C residue 89 type sequence F description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 8) chain C residue 127 type sequence T description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 9) chain C residue 128 type sequence A description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 10) chain C residue 131 type sequence G description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 11) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 12) chain C residue 183 type sequence H description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 13) chain C residue 184 type sequence Y description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 14) chain C residue 187 type sequence P description BINDING SITE FOR RESIDUE HEC C 701 source : AC1 15) chain C residue 30 type sequence W description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 16) chain C residue 33 type sequence G description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 17) chain C residue 36 type sequence L description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 18) chain C residue 96 type sequence H description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 19) chain C residue 97 type sequence M description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 20) chain C residue 99 type sequence K description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 21) chain C residue 105 type sequence S description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 22) chain C residue 113 type sequence L description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 23) chain C residue 117 type sequence G description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 24) chain C residue 120 type sequence I description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 25) chain C residue 194 type sequence V description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 26) chain C residue 197 type sequence H description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 27) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 28) chain C residue 206 type sequence S description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 29) chain C residue 207 type sequence S description BINDING SITE FOR RESIDUE HEC C 702 source : AC2 30) chain D residue 100 type sequence V description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 31) chain D residue 101 type sequence C description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 32) chain D residue 104 type sequence C description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 33) chain D residue 105 type sequence H description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 34) chain D residue 184 type sequence R description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 35) chain D residue 190 type sequence Y description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 36) chain D residue 191 type sequence I description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 37) chain D residue 218 type sequence F description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 38) chain D residue 223 type sequence I description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 39) chain D residue 224 type sequence A description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 40) chain D residue 225 type sequence M description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 41) chain D residue 228 type sequence V description BINDING SITE FOR RESIDUE HEC D 703 source : AC3 42) chain E residue 159 type sequence C description BINDING SITE FOR RESIDUE FES E 704 source : AC4 43) chain E residue 161 type sequence H description BINDING SITE FOR RESIDUE FES E 704 source : AC4 44) chain E residue 162 type sequence L description BINDING SITE FOR RESIDUE FES E 704 source : AC4 45) chain E residue 178 type sequence C description BINDING SITE FOR RESIDUE FES E 704 source : AC4 46) chain E residue 181 type sequence H description BINDING SITE FOR RESIDUE FES E 704 source : AC4 47) chain E residue 183 type sequence S description BINDING SITE FOR RESIDUE FES E 704 source : AC4 48) chain C residue 139 type sequence M description BINDING SITE FOR RESIDUE DBT C 705 source : AC5 49) chain C residue 143 type sequence G description BINDING SITE FOR RESIDUE DBT C 705 source : AC5 50) chain C residue 146 type sequence V description BINDING SITE FOR RESIDUE DBT C 705 source : AC5 51) chain C residue 147 type sequence I description BINDING SITE FOR RESIDUE DBT C 705 source : AC5 52) chain C residue 269 type sequence I description BINDING SITE FOR RESIDUE DBT C 705 source : AC5 53) chain C residue 271 type sequence P description BINDING SITE FOR RESIDUE DBT C 705 source : AC5 54) chain C residue 279 type sequence Y description BINDING SITE FOR RESIDUE DBT C 705 source : AC5 55) chain E residue 181 type sequence H description BINDING SITE FOR RESIDUE DBT C 705 source : AC5 56) chain C residue 16 type sequence Y description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 57) chain C residue 22 type sequence Q description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 58) chain C residue 26 type sequence I description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 59) chain C residue 34 type sequence S description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 60) chain C residue 44 type sequence I description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 61) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 62) chain C residue 206 type sequence S description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 63) chain C residue 221 type sequence M description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 64) chain C residue 229 type sequence D description BINDING SITE FOR RESIDUE UQ6 C 706 source : AC6 65) chain C residue 29 type sequence W description BINDING SITE FOR RESIDUE 3PE C 710 source : AC7 66) chain C residue 97 type sequence M description BINDING SITE FOR RESIDUE 3PE C 710 source : AC7 67) chain C residue 102 type sequence Y description BINDING SITE FOR RESIDUE 3PE C 710 source : AC7 68) chain C residue 103 type sequence Y description BINDING SITE FOR RESIDUE 3PE C 710 source : AC7 69) chain C residue 359 type sequence Y description BINDING SITE FOR RESIDUE 3PE C 710 source : AC7 70) chain G residue 82 type sequence E description BINDING SITE FOR RESIDUE 3PE C 710 source : AC7 71) chain H residue 51 type sequence R description BINDING SITE FOR RESIDUE 3PE C 710 source : AC7 72) chain H residue 52 type sequence F description BINDING SITE FOR RESIDUE 3PE C 710 source : AC7 73) chain C residue 3 type sequence F description BINDING SITE FOR RESIDUE 3PE C 711 source : AC8 74) chain C residue 7 type sequence N description BINDING SITE FOR RESIDUE 3PE C 711 source : AC8 75) chain C residue 9 type sequence Y description BINDING SITE FOR RESIDUE 3PE C 711 source : AC8 76) chain C residue 13 type sequence V description BINDING SITE FOR RESIDUE 3PE C 711 source : AC8 77) chain C residue 112 type sequence T description BINDING SITE FOR RESIDUE 3PE C 711 source : AC8 78) chain C residue 115 type sequence N description BINDING SITE FOR RESIDUE 3PE C 711 source : AC8 79) chain A residue 450 type sequence S description BINDING SITE FOR RESIDUE 3PH A 713 source : AC9 80) chain C residue 230 type sequence L description BINDING SITE FOR RESIDUE 3PH A 713 source : AC9 81) chain E residue 60 type sequence V description BINDING SITE FOR RESIDUE 3PH A 713 source : AC9 82) chain E residue 67 type sequence S description BINDING SITE FOR RESIDUE 3PH A 713 source : AC9 83) chain C residue 237 type sequence M description BINDING SITE FOR RESIDUE 3PH D 714 source : BC1 84) chain D residue 272 type sequence K description BINDING SITE FOR RESIDUE 3PH D 714 source : BC1 85) chain D residue 273 type sequence T description BINDING SITE FOR RESIDUE 3PH D 714 source : BC1 86) chain D residue 276 type sequence I description BINDING SITE FOR RESIDUE 3PH D 714 source : BC1 87) chain E residue 70 type sequence G description BINDING SITE FOR RESIDUE 3PH D 714 source : BC1 88) chain E residue 73 type sequence S description BINDING SITE FOR RESIDUE 3PH D 714 source : BC1 89) chain C residue 253 type sequence H description BINDING SITE FOR RESIDUE PC1 D 715 source : BC2 90) chain C residue 268 type sequence S description BINDING SITE FOR RESIDUE PC1 D 715 source : BC2 91) chain C residue 273 type sequence W description BINDING SITE FOR RESIDUE PC1 D 715 source : BC2 92) chain C residue 337 type sequence G description BINDING SITE FOR RESIDUE PC1 D 715 source : BC2 93) chain D residue 185 type sequence H description BINDING SITE FOR RESIDUE PC1 D 715 source : BC2 94) chain A residue 427 type sequence W description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 95) chain A residue 428 type sequence D description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 96) chain A residue 453 type sequence S description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 97) chain A residue 454 type sequence M description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 98) chain A residue 455 type sequence M description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 99) chain A residue 456 type sequence R description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 100) chain E residue 57 type sequence Y description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 101) chain E residue 68 type sequence S description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 102) chain I residue 14 type sequence N description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 103) chain I residue 15 type sequence A description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 104) chain I residue 16 type sequence V description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 105) chain I residue 17 type sequence F description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 106) chain I residue 18 type sequence V description BINDING SITE FOR RESIDUE UMQ A 721 source : BC3 107) chain C residue 27 type sequence N description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 108) chain C residue 28 type sequence Y description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 109) chain C residue 32 type sequence M description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 110) chain C residue 95 type sequence M description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 111) chain C residue 235 type sequence L description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 112) chain D residue 281 type sequence Y description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 113) chain D residue 288 type sequence K description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 114) chain D residue 289 type sequence K description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 115) chain G residue 85 type sequence H description BINDING SITE FOR RESIDUE CDL D 731 source : BC4 116) chain E residue 181 type catalytic sequence H description 208 source MCSA : MCSA1 117) chain C residue 206 type catalytic sequence S description 208 source MCSA : MCSA1 118) chain C residue 228 type catalytic sequence K description 208 source MCSA : MCSA1 119) chain C residue 229 type catalytic sequence D description 208 source MCSA : MCSA1 120) chain C residue 272 type catalytic sequence E description 208 source MCSA : MCSA1 121) chain B residue 37-59 type prosite sequence GGSRYATKDGVAHLLNRFNFQNT description INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT source prosite : PS00143 122) chain I residue 19-44 type TRANSMEM sequence GTIFAGAFVFQTVFDTAITSWYENHN description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 123) chain C residue 103-110 type TRANSMEM sequence YGSYRSPR description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 124) chain C residue 205-223 type TRANSMEM sequence GSSNPLGITGNLDRIPMHS description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 125) chain C residue 309-319 type TRANSMEM sequence DRSVVRGNTFK description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 126) chain C residue 365-385 type TRANSMEM sequence IIVPVISTIENVLFYIGRVNK description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 127) chain H residue 50-80 type TRANSMEM sequence RRFKSQFLYVLIPAGIYWYWWKNGNEYNEFL description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 128) 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 129) 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 130) 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 131) 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 132) 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 133) 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 134) 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 135) chain H 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 136) chain D residue 104 type TOPO_DOM sequence C description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI3 137) 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 138) 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 139) 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 140) 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 141) 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 142) 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 143) 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_FI5 144) chain C residue 96 type BINDING sequence H 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_FI5 145) chain C residue 183 type BINDING sequence H 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_FI5 146) chain C residue 197 type BINDING sequence H 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_FI5 147) chain C residue 202 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI6

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