eF-site ID 1kyo-C PDB Code 1kyo Chain C click to enlarge Title YEAST CYTOCHROME BC1 COMPLEX WITH BOUND SUBSTRATE CYTOCHROME C Classification OXIDOREDUCTASE/ELECTRON TRANSPORT Compound UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence C:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK Description Functional site 1) chain C residue 43 type sequence Q description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 2) chain C residue 47 type sequence G description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 3) chain C residue 48 type sequence I description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 4) chain C residue 50 type sequence M description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 5) chain C residue 51 type sequence A description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 6) chain C residue 79 type sequence R description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 7) chain C residue 82 type sequence H description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 8) chain C residue 83 type sequence A description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 9) chain C residue 127 type sequence T description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 10) chain C residue 128 type sequence A description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 11) chain C residue 131 type sequence G description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 12) chain C residue 132 type sequence Y description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 13) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 14) chain C residue 183 type sequence H description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 15) chain C residue 184 type sequence Y description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 16) chain C residue 187 type sequence P description BINDING SITE FOR RESIDUE HEC C 501 source : AC1 17) chain C residue 30 type sequence W description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 18) chain C residue 33 type sequence G description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 19) chain C residue 96 type sequence H description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 20) chain C residue 97 type sequence M description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 21) chain C residue 99 type sequence K description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 22) chain C residue 105 type sequence S description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 23) chain C residue 113 type sequence L description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 24) chain C residue 117 type sequence G description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 25) chain C residue 118 type sequence V description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 26) chain C residue 120 type sequence I description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 27) chain C residue 197 type sequence H description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 28) chain C residue 201 type sequence L description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 29) chain C residue 206 type sequence S description BINDING SITE FOR RESIDUE HEC C 502 source : AC2 30) chain C residue 207 type sequence S description BINDING SITE FOR RESIDUE HEC 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 126 type sequence A 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 147 type sequence I description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 36) chain C residue 165 type sequence L description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 37) chain C residue 270 type sequence V description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 38) chain C residue 271 type sequence P description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 39) chain C residue 272 type sequence E description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 40) chain C residue 278 type sequence F description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 41) chain C residue 279 type sequence Y description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 42) chain C residue 295 type sequence M description BINDING SITE FOR RESIDUE SMA C 505 source : AC5 43) chain C residue 206 type catalytic sequence S description 208 source MCSA : MCSA1 44) chain C residue 228 type catalytic sequence K description 208 source MCSA : MCSA1 45) chain C residue 229 type catalytic sequence D description 208 source MCSA : MCSA1 46) chain C residue 272 type catalytic sequence E description 208 source MCSA : MCSA1 47) chain C residue 205-223 type BINDING sequence GSSNPLGITGNLDRIPMHS description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 48) chain C residue 309-319 type BINDING sequence DRSVVRGNTFK description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 49) chain C residue 365-385 type BINDING sequence IIVPVISTIENVLFYIGRVNK description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 50) chain C residue 111-135 type BINDING sequence VTLWNVGVIIFTLTIATAFLGYCCV description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 51) chain C residue 173-204 type BINDING sequence NPTIQRFFALHYLVPFIIAAMVIMHLMALHIH description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 52) chain C residue 224-246 type BINDING sequence YFIFKDLVTVFLFMLILALFVFY description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 53) chain C residue 288-308 type BINDING sequence KLLGVITMFAAILVLLVLPFT description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 54) chain C residue 320-340 type BINDING sequence VLSKFFFFIFVFNFVLLGQIG description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 55) chain C residue 348-364 type BINDING sequence YVLMGQIATFIYFAYFL description axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI2 56) chain C residue 247-287 type MOD_RES sequence SPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIP D description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 57) chain C residue 341-347 type MOD_RES sequence ACHVEVP description N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO source Swiss-Prot : SWS_FT_FI3 58) 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 59) 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

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