eF-site ID 1kb9-C PDB Code 1kb9 Chain C click to enlarge Title YEAST CYTOCHROME BC1 COMPLEX Classification OXIDOREDUCTASE/ELECTRON TRANSPORT Compound UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (1KB9) Sequence C:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK Description (1)  UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2, CYTOCHROME B, CYTOCHROME C1, HEME PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN, HEAVY CHAIN (VH) OF FV-FRAGMENT, LIGHT CHAIN (VL) OF FV-FRAGMENT, PROTOPORPHYRIN IX CONTAINING FE, FE2/S2 (INORGANIC) CLUSTER, ESTRIOL 3-(B-D-GLUCURONIDE), 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL, 2-[(HYDROXY{[(2R,3R,5S,6R)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXYL]OXY}PHOSPHORYL)OXY]-1-[(PALMITOYLOXY)METHYL]ETHYL HEPTADECANOATE, 5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOBUTYL-HEXANOIC ACID, 9-(4-HYDROXY-3-(HYDROXYMETHYL)BUT-1-YL)GUANINE, 5-OXOPROLINE, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE Functional site 1) chain C residue 40 type sequence L description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 2) chain C residue 43 type sequence Q description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 3) chain C residue 47 type sequence G description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 4) chain C residue 48 type sequence I description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 5) chain C residue 50 type sequence M description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 6) chain C residue 51 type sequence A description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 7) chain C residue 79 type sequence R description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 8) chain C residue 82 type sequence H description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 9) chain C residue 89 type sequence F description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 10) chain C residue 127 type sequence T description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 11) chain C residue 128 type sequence A description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 12) chain C residue 131 type sequence G description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 13) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 14) chain C residue 183 type sequence H description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 15) chain C residue 184 type sequence Y description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 16) chain C residue 187 type sequence P description BINDING SITE FOR RESIDUE HEM C 501 source : AC1 17) chain C residue 30 type sequence W description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 18) chain C residue 33 type sequence G description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 19) chain C residue 36 type sequence L description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 20) chain C residue 96 type sequence H description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 21) chain C residue 99 type sequence K description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 22) chain C residue 105 type sequence S description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 23) chain C residue 113 type sequence L description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 24) chain C residue 117 type sequence G description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 25) chain C residue 118 type sequence V description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 26) chain C residue 120 type sequence I description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 27) chain C residue 197 type sequence H description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 28) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 29) chain C residue 206 type sequence S description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 30) chain C residue 207 type sequence S description BINDING SITE FOR RESIDUE HEM C 502 source : AC2 31) chain C residue 125 type sequence I description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 32) chain C residue 129 type sequence F description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 33) chain C residue 143 type sequence G description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 34) chain C residue 146 type sequence V description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 35) chain C residue 271 type sequence P description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 36) chain C residue 272 type sequence E description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 37) chain C residue 275 type sequence L description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 38) chain C residue 279 type sequence Y description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 39) chain C residue 295 type sequence M description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 40) chain C residue 296 type sequence F description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 41) chain C residue 16 type sequence Y description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC6 42) chain C residue 22 type sequence Q description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC6 43) chain C residue 40 type sequence L description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC6 44) chain C residue 44 type sequence I description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC6 45) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC6 46) chain C residue 206 type sequence S description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC6 47) chain C residue 221 type sequence M description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC6 48) chain C residue 229 type sequence D description BINDING SITE FOR RESIDUE UQ6 C 506 source : AC6 49) chain C residue 74 type sequence N description BINDING SITE FOR RESIDUE PIE C 508 source : AC7 50) chain C residue 237 type sequence M description BINDING SITE FOR RESIDUE PIE C 508 source : AC7 51) chain C residue 245 type sequence F description BINDING SITE FOR RESIDUE PIE C 508 source : AC7 52) chain C residue 98 type sequence A description BINDING SITE FOR RESIDUE PEF C 510 source : AC8 53) chain C residue 102 type sequence Y description BINDING SITE FOR RESIDUE PEF C 510 source : AC8 54) chain C residue 103 type sequence Y description BINDING SITE FOR RESIDUE PEF C 510 source : AC8 55) chain C residue 326 type sequence F description BINDING SITE FOR RESIDUE PEF C 510 source : AC8 56) chain C residue 327 type sequence F description BINDING SITE FOR RESIDUE PEF C 510 source : AC8 57) chain C residue 329 type sequence F description BINDING SITE FOR RESIDUE PEF C 510 source : AC8 58) chain C residue 333 type sequence F description BINDING SITE FOR RESIDUE PEF C 510 source : AC8 59) chain C residue 27 type sequence N description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 60) chain C residue 28 type sequence Y description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 61) chain C residue 29 type sequence W description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 62) chain C residue 32 type sequence M description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 63) chain C residue 95 type sequence M description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 64) chain C residue 231 type sequence V description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 65) chain C residue 235 type sequence L description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 66) chain C residue 3 type sequence F description BINDING SITE FOR RESIDUE PEF C 513 source : BC1 67) chain C residue 7 type sequence N description BINDING SITE FOR RESIDUE PEF C 513 source : BC1 68) chain C residue 13 type sequence V description BINDING SITE FOR RESIDUE PEF C 513 source : BC1 69) chain C residue 112 type sequence T description BINDING SITE FOR RESIDUE PEF C 513 source : BC1 70) chain C residue 115 type sequence N description BINDING SITE FOR RESIDUE PEF C 513 source : BC1 71) chain C residue 222 type sequence H description BINDING SITE FOR RESIDUE PCF A 514 source : BC2 72) chain C residue 206 type catalytic sequence S description 208 source MCSA : MCSA1 73) chain C residue 228 type catalytic sequence K description 208 source MCSA : MCSA1 74) chain C residue 229 type catalytic sequence D description 208 source MCSA : MCSA1 75) chain C residue 272 type catalytic sequence E description 208 source MCSA : MCSA1 76) 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 77) 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 78) 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 79) chain C residue 202 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P00157 source Swiss-Prot : SWS_FT_FI6 80) 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 81) 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 82) 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 83) 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 84) 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 85) 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 86) 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 87) 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 88) 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 89) 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 90) 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 91) 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 92) 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

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