eF-site ID 4pd4-ABCDEFGHIJK PDB Code 4pd4 Chain A, B, C, D, E, F, G, H, I, J, K click to enlarge Title Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action Classification OXIDOREDUCTASE/INHIBITOR Compound Cytochrome b-c1 complex subunit 1, mitochondrial Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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 Description Functional site 1) chain A residue 427 type sequence W description binding site for residue UMQ A 501 source : AC1 2) chain A residue 428 type sequence D description binding site for residue UMQ A 501 source : AC1 3) chain A residue 453 type sequence S description binding site for residue UMQ A 501 source : AC1 4) chain A residue 454 type sequence M description binding site for residue UMQ A 501 source : AC1 5) chain A residue 455 type sequence M description binding site for residue UMQ A 501 source : AC1 6) chain A residue 456 type sequence R description binding site for residue UMQ A 501 source : AC1 7) chain E residue 57 type sequence Y description binding site for residue UMQ A 501 source : AC1 8) chain E residue 68 type sequence S description binding site for residue UMQ A 501 source : AC1 9) chain I residue 14 type sequence N description binding site for residue UMQ A 501 source : AC1 10) chain I residue 15 type sequence A description binding site for residue UMQ A 501 source : AC1 11) chain I residue 16 type sequence V description binding site for residue UMQ A 501 source : AC1 12) chain I residue 17 type sequence F description binding site for residue UMQ A 501 source : AC1 13) chain I residue 18 type sequence V description binding site for residue UMQ A 501 source : AC1 14) chain A residue 450 type sequence S description binding site for residue 3PH A 502 source : AC2 15) chain C residue 222 type sequence H description binding site for residue 3PH A 502 source : AC2 16) chain C residue 226 type sequence I description binding site for residue 3PH A 502 source : AC2 17) chain E residue 67 type sequence S description binding site for residue 3PH A 502 source : AC2 18) chain C residue 43 type sequence Q description binding site for residue HEM C 4001 source : AC3 19) chain C residue 44 type sequence I description binding site for residue HEM C 4001 source : AC3 20) chain C residue 47 type sequence G description binding site for residue HEM C 4001 source : AC3 21) chain C residue 48 type sequence I description binding site for residue HEM C 4001 source : AC3 22) chain C residue 50 type sequence M description binding site for residue HEM C 4001 source : AC3 23) chain C residue 51 type sequence A description binding site for residue HEM C 4001 source : AC3 24) chain C residue 79 type sequence R description binding site for residue HEM C 4001 source : AC3 25) chain C residue 82 type sequence H description binding site for residue HEM C 4001 source : AC3 26) chain C residue 83 type sequence A description binding site for residue HEM C 4001 source : AC3 27) chain C residue 127 type sequence T description binding site for residue HEM C 4001 source : AC3 28) chain C residue 128 type sequence A description binding site for residue HEM C 4001 source : AC3 29) chain C residue 131 type sequence G description binding site for residue HEM C 4001 source : AC3 30) chain C residue 132 type sequence Y description binding site for residue HEM C 4001 source : AC3 31) chain C residue 135 type sequence V description binding site for residue HEM C 4001 source : AC3 32) chain C residue 180 type sequence F description binding site for residue HEM C 4001 source : AC3 33) chain C residue 183 type sequence H description binding site for residue HEM C 4001 source : AC3 34) chain C residue 184 type sequence Y description binding site for residue HEM C 4001 source : AC3 35) chain C residue 187 type sequence P description binding site for residue HEM C 4001 source : AC3 36) chain C residue 30 type sequence W description binding site for residue HEM C 4002 source : AC4 37) chain C residue 33 type sequence G description binding site for residue HEM C 4002 source : AC4 38) chain C residue 34 type sequence S description binding site for residue HEM C 4002 source : AC4 39) chain C residue 36 type sequence L description binding site for residue HEM C 4002 source : AC4 40) chain C residue 96 type sequence H description binding site for residue HEM C 4002 source : AC4 41) chain C residue 97 type sequence M description binding site for residue HEM C 4002 source : AC4 42) chain C residue 99 type sequence K description binding site for residue HEM C 4002 source : AC4 43) chain C residue 105 type sequence S description binding site for residue HEM C 4002 source : AC4 44) chain C residue 113 type sequence L description binding site for residue HEM C 4002 source : AC4 45) chain C residue 114 type sequence W description binding site for residue HEM C 4002 source : AC4 46) chain C residue 117 type sequence G description binding site for residue HEM C 4002 source : AC4 47) chain C residue 118 type sequence V description binding site for residue HEM C 4002 source : AC4 48) chain C residue 120 type sequence I description binding site for residue HEM C 4002 source : AC4 49) chain C residue 194 type sequence V description binding site for residue HEM C 4002 source : AC4 50) chain C residue 197 type sequence H description binding site for residue HEM C 4002 source : AC4 51) chain C residue 201 type sequence L description binding site for residue HEM C 4002 source : AC4 52) chain C residue 206 type sequence S description binding site for residue HEM C 4002 source : AC4 53) chain C residue 207 type sequence S description binding site for residue HEM C 4002 source : AC4 54) chain C residue 129 type sequence F description binding site for residue AOQ C 4003 source : AC5 55) chain C residue 139 type sequence M description binding site for residue AOQ C 4003 source : AC5 56) chain C residue 143 type sequence G description binding site for residue AOQ C 4003 source : AC5 57) chain C residue 146 type sequence V description binding site for residue AOQ C 4003 source : AC5 58) chain C residue 147 type sequence I description binding site for residue AOQ C 4003 source : AC5 59) chain C residue 269 type sequence I description binding site for residue AOQ C 4003 source : AC5 60) chain C residue 271 type sequence P description binding site for residue AOQ C 4003 source : AC5 61) chain C residue 275 type sequence L description binding site for residue AOQ C 4003 source : AC5 62) chain C residue 279 type sequence Y description binding site for residue AOQ C 4003 source : AC5 63) chain C residue 299 type sequence I description binding site for residue AOQ C 4003 source : AC5 64) chain E residue 181 type sequence H description binding site for residue AOQ C 4003 source : AC5 65) chain C residue 3 type sequence F description binding site for residue 3PE C 4004 source : AC6 66) chain C residue 7 type sequence N description binding site for residue 3PE C 4004 source : AC6 67) chain C residue 9 type sequence Y description binding site for residue 3PE C 4004 source : AC6 68) chain C residue 10 type sequence L description binding site for residue 3PE C 4004 source : AC6 69) chain C residue 112 type sequence T description binding site for residue 3PE C 4004 source : AC6 70) chain C residue 115 type sequence N description binding site for residue 3PE C 4004 source : AC6 71) chain C residue 116 type sequence V description binding site for residue 3PE C 4004 source : AC6 72) chain C residue 204 type sequence H description binding site for residue 3PE C 4004 source : AC6 73) chain C residue 16 type sequence Y description binding site for residue UQ6 C 4005 source : AC7 74) chain C residue 22 type sequence Q description binding site for residue UQ6 C 4005 source : AC7 75) chain C residue 34 type sequence S description binding site for residue UQ6 C 4005 source : AC7 76) chain C residue 48 type sequence I description binding site for residue UQ6 C 4005 source : AC7 77) chain C residue 182 type sequence L description binding site for residue UQ6 C 4005 source : AC7 78) chain C residue 185 type sequence L description binding site for residue UQ6 C 4005 source : AC7 79) chain C residue 191 type sequence A description binding site for residue UQ6 C 4005 source : AC7 80) chain C residue 201 type sequence L description binding site for residue UQ6 C 4005 source : AC7 81) chain C residue 206 type sequence S description binding site for residue UQ6 C 4005 source : AC7 82) chain C residue 221 type sequence M description binding site for residue UQ6 C 4005 source : AC7 83) chain C residue 229 type sequence D description binding site for residue UQ6 C 4005 source : AC7 84) chain C residue 29 type sequence W description binding site for residue 3PH C 4006 source : AC8 85) chain C residue 95 type sequence M description binding site for residue 3PH C 4006 source : AC8 86) chain C residue 97 type sequence M description binding site for residue 3PH C 4006 source : AC8 87) chain C residue 98 type sequence A description binding site for residue 3PH C 4006 source : AC8 88) chain C residue 102 type sequence Y description binding site for residue 3PH C 4006 source : AC8 89) chain C residue 103 type sequence Y description binding site for residue 3PH C 4006 source : AC8 90) chain C residue 302 type sequence L description binding site for residue 3PH C 4006 source : AC8 91) chain C residue 317 type sequence T description binding site for residue 3PH C 4006 source : AC8 92) chain C residue 333 type sequence F description binding site for residue 3PH C 4006 source : AC8 93) chain D residue 100 type sequence V description binding site for residue HEM D 401 source : AC9 94) chain D residue 101 type sequence C description binding site for residue HEM D 401 source : AC9 95) chain D residue 104 type sequence C description binding site for residue HEM D 401 source : AC9 96) chain D residue 105 type sequence H description binding site for residue HEM D 401 source : AC9 97) chain D residue 169 type sequence N description binding site for residue HEM D 401 source : AC9 98) chain D residue 172 type sequence A description binding site for residue HEM D 401 source : AC9 99) chain D residue 175 type sequence P description binding site for residue HEM D 401 source : AC9 100) chain D residue 180 type sequence I description binding site for residue HEM D 401 source : AC9 101) chain D residue 184 type sequence R description binding site for residue HEM D 401 source : AC9 102) chain D residue 190 type sequence Y description binding site for residue HEM D 401 source : AC9 103) chain D residue 191 type sequence I description binding site for residue HEM D 401 source : AC9 104) chain D residue 195 type sequence L description binding site for residue HEM D 401 source : AC9 105) chain D residue 218 type sequence F description binding site for residue HEM D 401 source : AC9 106) chain D residue 225 type sequence M description binding site for residue HEM D 401 source : AC9 107) chain D residue 228 type sequence V description binding site for residue HEM D 401 source : AC9 108) chain D residue 251 type sequence V description binding site for residue HEM D 401 source : AC9 109) chain E residue 159 type sequence C description binding site for residue FES E 301 source : AD1 110) chain E residue 161 type sequence H description binding site for residue FES E 301 source : AD1 111) chain E residue 162 type sequence L description binding site for residue FES E 301 source : AD1 112) chain E residue 178 type sequence C description binding site for residue FES E 301 source : AD1 113) chain E residue 180 type sequence C description binding site for residue FES E 301 source : AD1 114) chain E residue 181 type sequence H description binding site for residue FES E 301 source : AD1 115) chain E residue 183 type sequence S description binding site for residue FES E 301 source : AD1 116) chain C residue 42 type sequence I description binding site for residue 3PH E 302 source : AD2 117) chain C residue 237 type sequence M description binding site for residue 3PH E 302 source : AD2 118) chain D residue 269 type sequence L description binding site for residue 3PH E 302 source : AD2 119) chain D residue 272 type sequence K description binding site for residue 3PH E 302 source : AD2 120) chain D residue 273 type sequence T description binding site for residue 3PH E 302 source : AD2 121) chain D residue 276 type sequence I description binding site for residue 3PH E 302 source : AD2 122) chain E residue 70 type sequence G description binding site for residue 3PH E 302 source : AD2 123) chain E residue 71 type sequence A description binding site for residue 3PH E 302 source : AD2 124) chain E residue 73 type sequence S description binding site for residue 3PH E 302 source : AD2 125) chain E residue 74 type sequence T description binding site for residue 3PH E 302 source : AD2 126) chain E residue 77 type sequence T description binding site for residue 3PH E 302 source : AD2 127) chain B residue 37-59 type prosite sequence GGSRYATKDGVAHLLNRFNFQNT description INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT source prosite : PS00143 128) chain I residue 2-17 type TOPO_DOM sequence SFSSLYKTFFKRNAVF description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 129) 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 130) 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 131) 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 132) 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 133) chain I residue 18-43 type TRANSMEM sequence VGTIFAGAFVFQTVFDTAITSWYENH description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 134) 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 135) chain C residue 111-135 type TRANSMEM sequence VTLWNVGVIIFILTIATAFLGYCCV description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI2 136) 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 137) 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 138) 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 139) 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 140) 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 141) 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 142) 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 143) 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 144) 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 145) 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 146) 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 147) 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 148) 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 149) 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 150) 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 151) 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 152) 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 153) chain E residue 181 type catalytic sequence H description 208 source MCSA : MCSA1 154) chain C residue 206 type catalytic sequence S description 208 source MCSA : MCSA1 155) chain C residue 228 type catalytic sequence K description 208 source MCSA : MCSA1 156) chain C residue 229 type catalytic sequence D description 208 source MCSA : MCSA1 157) chain C residue 272 type catalytic sequence E description 208 source MCSA : MCSA1 158) 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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