eF-site ID 4pd4-C PDB Code 4pd4 Chain C 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 C:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK Description Functional site 1) chain C residue 222 type sequence H description binding site for residue 3PH A 502 source : AC2 2) chain C residue 226 type sequence I description binding site for residue 3PH A 502 source : AC2 3) chain C residue 43 type sequence Q description binding site for residue HEM C 4001 source : AC3 4) chain C residue 44 type sequence I description binding site for residue HEM C 4001 source : AC3 5) chain C residue 47 type sequence G description binding site for residue HEM C 4001 source : AC3 6) chain C residue 48 type sequence I description binding site for residue HEM C 4001 source : AC3 7) chain C residue 50 type sequence M description binding site for residue HEM C 4001 source : AC3 8) chain C residue 51 type sequence A description binding site for residue HEM C 4001 source : AC3 9) chain C residue 79 type sequence R description binding site for residue HEM C 4001 source : AC3 10) chain C residue 82 type sequence H description binding site for residue HEM C 4001 source : AC3 11) chain C residue 83 type sequence A description binding site for residue HEM C 4001 source : AC3 12) chain C residue 127 type sequence T description binding site for residue HEM C 4001 source : AC3 13) chain C residue 128 type sequence A description binding site for residue HEM C 4001 source : AC3 14) chain C residue 131 type sequence G description binding site for residue HEM C 4001 source : AC3 15) chain C residue 132 type sequence Y description binding site for residue HEM C 4001 source : AC3 16) chain C residue 135 type sequence V description binding site for residue HEM C 4001 source : AC3 17) chain C residue 180 type sequence F description binding site for residue HEM C 4001 source : AC3 18) chain C residue 183 type sequence H description binding site for residue HEM C 4001 source : AC3 19) chain C residue 184 type sequence Y description binding site for residue HEM C 4001 source : AC3 20) chain C residue 187 type sequence P description binding site for residue HEM C 4001 source : AC3 21) chain C residue 30 type sequence W description binding site for residue HEM C 4002 source : AC4 22) chain C residue 33 type sequence G description binding site for residue HEM C 4002 source : AC4 23) chain C residue 34 type sequence S description binding site for residue HEM C 4002 source : AC4 24) chain C residue 36 type sequence L description binding site for residue HEM C 4002 source : AC4 25) chain C residue 96 type sequence H description binding site for residue HEM C 4002 source : AC4 26) chain C residue 97 type sequence M description binding site for residue HEM C 4002 source : AC4 27) chain C residue 99 type sequence K description binding site for residue HEM C 4002 source : AC4 28) chain C residue 105 type sequence S description binding site for residue HEM C 4002 source : AC4 29) chain C residue 113 type sequence L description binding site for residue HEM C 4002 source : AC4 30) chain C residue 114 type sequence W description binding site for residue HEM C 4002 source : AC4 31) chain C residue 117 type sequence G description binding site for residue HEM C 4002 source : AC4 32) chain C residue 118 type sequence V description binding site for residue HEM C 4002 source : AC4 33) chain C residue 120 type sequence I description binding site for residue HEM C 4002 source : AC4 34) chain C residue 194 type sequence V description binding site for residue HEM C 4002 source : AC4 35) chain C residue 197 type sequence H description binding site for residue HEM C 4002 source : AC4 36) chain C residue 201 type sequence L description binding site for residue HEM C 4002 source : AC4 37) chain C residue 206 type sequence S description binding site for residue HEM C 4002 source : AC4 38) chain C residue 207 type sequence S description binding site for residue HEM C 4002 source : AC4 39) chain C residue 129 type sequence F description binding site for residue AOQ C 4003 source : AC5 40) chain C residue 139 type sequence M description binding site for residue AOQ C 4003 source : AC5 41) chain C residue 143 type sequence G description binding site for residue AOQ C 4003 source : AC5 42) chain C residue 146 type sequence V description binding site for residue AOQ C 4003 source : AC5 43) chain C residue 147 type sequence I description binding site for residue AOQ C 4003 source : AC5 44) chain C residue 269 type sequence I description binding site for residue AOQ C 4003 source : AC5 45) chain C residue 271 type sequence P description binding site for residue AOQ C 4003 source : AC5 46) chain C residue 275 type sequence L description binding site for residue AOQ C 4003 source : AC5 47) chain C residue 279 type sequence Y description binding site for residue AOQ C 4003 source : AC5 48) chain C residue 299 type sequence I description binding site for residue AOQ C 4003 source : AC5 49) chain C residue 3 type sequence F description binding site for residue 3PE C 4004 source : AC6 50) chain C residue 7 type sequence N description binding site for residue 3PE C 4004 source : AC6 51) chain C residue 9 type sequence Y description binding site for residue 3PE C 4004 source : AC6 52) chain C residue 10 type sequence L description binding site for residue 3PE C 4004 source : AC6 53) chain C residue 112 type sequence T description binding site for residue 3PE C 4004 source : AC6 54) chain C residue 115 type sequence N description binding site for residue 3PE C 4004 source : AC6 55) chain C residue 116 type sequence V description binding site for residue 3PE C 4004 source : AC6 56) chain C residue 204 type sequence H description binding site for residue 3PE C 4004 source : AC6 57) chain C residue 16 type sequence Y description binding site for residue UQ6 C 4005 source : AC7 58) chain C residue 22 type sequence Q description binding site for residue UQ6 C 4005 source : AC7 59) chain C residue 34 type sequence S description binding site for residue UQ6 C 4005 source : AC7 60) chain C residue 48 type sequence I description binding site for residue UQ6 C 4005 source : AC7 61) chain C residue 182 type sequence L description binding site for residue UQ6 C 4005 source : AC7 62) chain C residue 185 type sequence L description binding site for residue UQ6 C 4005 source : AC7 63) chain C residue 191 type sequence A description binding site for residue UQ6 C 4005 source : AC7 64) chain C residue 201 type sequence L description binding site for residue UQ6 C 4005 source : AC7 65) chain C residue 206 type sequence S description binding site for residue UQ6 C 4005 source : AC7 66) chain C residue 221 type sequence M description binding site for residue UQ6 C 4005 source : AC7 67) chain C residue 229 type sequence D description binding site for residue UQ6 C 4005 source : AC7 68) chain C residue 29 type sequence W description binding site for residue 3PH C 4006 source : AC8 69) chain C residue 95 type sequence M description binding site for residue 3PH C 4006 source : AC8 70) chain C residue 97 type sequence M description binding site for residue 3PH C 4006 source : AC8 71) chain C residue 98 type sequence A description binding site for residue 3PH C 4006 source : AC8 72) chain C residue 102 type sequence Y description binding site for residue 3PH C 4006 source : AC8 73) chain C residue 103 type sequence Y description binding site for residue 3PH C 4006 source : AC8 74) chain C residue 302 type sequence L description binding site for residue 3PH C 4006 source : AC8 75) chain C residue 317 type sequence T description binding site for residue 3PH C 4006 source : AC8 76) chain C residue 333 type sequence F description binding site for residue 3PH C 4006 source : AC8 77) chain C residue 42 type sequence I description binding site for residue 3PH E 302 source : AD2 78) chain C residue 237 type sequence M description binding site for residue 3PH E 302 source : AD2 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 103-110 type TOPO_DOM sequence YGSYRSPR description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI1 84) 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 85) 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 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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 93) 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 94) 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 95) 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 96) 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 97) 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 98) 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 99) 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

Display surface Download Links