eF-site ID 1kyo-N PDB Code 1kyo Chain N 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 N:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK Description Functional site 1) chain N residue 43 type sequence Q description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 2) chain N residue 47 type sequence G description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 3) chain N residue 48 type sequence I description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 4) chain N residue 50 type sequence M description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 5) chain N residue 79 type sequence R description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 6) chain N residue 82 type sequence H description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 7) chain N residue 83 type sequence A description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 8) chain N residue 89 type sequence F description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 9) chain N residue 128 type sequence A description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 10) chain N residue 131 type sequence G description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 11) chain N residue 132 type sequence Y description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 12) chain N residue 135 type sequence V description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 13) chain N residue 183 type sequence H description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 14) chain N residue 184 type sequence Y description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 15) chain N residue 187 type sequence P description BINDING SITE FOR RESIDUE HEC N 521 source : AC6 16) chain N residue 30 type sequence W description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 17) chain N residue 33 type sequence G description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 18) chain N residue 36 type sequence L description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 19) chain N residue 96 type sequence H description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 20) chain N residue 99 type sequence K description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 21) chain N residue 105 type sequence S description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 22) chain N residue 113 type sequence L description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 23) chain N residue 114 type sequence W description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 24) chain N residue 117 type sequence G description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 25) chain N residue 194 type sequence V description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 26) chain N residue 197 type sequence H description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 27) chain N residue 201 type sequence L description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 28) chain N residue 206 type sequence S description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 29) chain N residue 207 type sequence S description BINDING SITE FOR RESIDUE HEC N 522 source : AC7 30) chain N residue 122 type sequence T description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 31) chain N residue 125 type sequence I description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 32) chain N residue 126 type sequence A description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 33) chain N residue 129 type sequence F description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 34) chain N residue 130 type sequence L description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 35) chain N residue 139 type sequence M description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 36) chain N residue 146 type sequence V description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 37) chain N residue 147 type sequence I description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 38) chain N residue 269 type sequence I description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 39) chain N residue 271 type sequence P description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 40) chain N residue 272 type sequence E description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 41) chain N residue 279 type sequence Y description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 42) chain N residue 295 type sequence M description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 43) chain N residue 296 type sequence F description BINDING SITE FOR RESIDUE SMA N 525 source : BC1 44) chain N residue 206 type catalytic sequence S description 208 source MCSA : MCSA2 45) chain N residue 228 type catalytic sequence K description 208 source MCSA : MCSA2 46) chain N residue 229 type catalytic sequence D description 208 source MCSA : MCSA2 47) chain N residue 272 type catalytic sequence E description 208 source MCSA : MCSA2 48) chain N 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 49) chain N residue 1-27 type BINDING sequence MAFRKSNVYLSLVNSYIIDSPQPSSIN 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 N residue 103-110 type BINDING sequence YGSYRSPR description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 51) chain N 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 52) chain N 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 53) chain N residue 75-102 type BINDING sequence GYILRYLHANGASFFFMVMFMHMAKGLY 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 N 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 55) chain N 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 56) chain N 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 57) chain N 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 58) chain N 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 59) chain N 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 60) chain N residue 28-51 type BINDING sequence YWWNMGSLLGLCLVIQIVTGIFMA 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 61) chain N residue 52-74 type MOD_RES sequence MHYSSNIELAFSSVEHIMRDVHN 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 62) chain N residue 136-172 type MOD_RES sequence YGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVS 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 63) chain N 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 64) chain N 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 65) chain N residue 82 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 66) chain N 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 67) chain N 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 68) chain N 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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