eF-site ID 3cxh-N PDB Code 3cxh Chain N click to enlarge Title Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a minimal core interface for electron transfer. Classification OXIDOREDUCTASE Compound Cytochrome b-c1 complex subunit 1, mitochondrial Source ORGANISM_COMMON: yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence N:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF AYFLIIVPVISTIENVLFYIGRVNK Description Functional site 1) chain N residue 206 type catalytic sequence S description 208 source MCSA : MCSA2 2) chain N residue 228 type catalytic sequence K description 208 source MCSA : MCSA2 3) chain N residue 229 type catalytic sequence D description 208 source MCSA : MCSA2 4) chain N residue 272 type catalytic sequence E description 208 source MCSA : MCSA2 5) 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 6) 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 7) 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 8) 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 9) chain N residue 365-385 type BINDING sequence IIVPVISTIENVLFYIGRVNK description covalent => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI1 10) chain N residue 1-27 type BINDING sequence MAFRKSNVYLSLVNSYIIDSPQPSSIN description covalent => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI1 11) chain N residue 103-110 type BINDING sequence YGSYRSPR description covalent => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI1 12) chain N residue 205-223 type BINDING sequence GSSNPLGITGNLDRIPMHS description covalent => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI1 13) chain N residue 309-319 type BINDING sequence DRSVVRGNTFK description covalent => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI1 14) chain N residue 75-102 type BINDING sequence GYILRYLHANGASFFFMVMFMHMAKGLY description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI2 15) chain N residue 111-135 type BINDING sequence VTLWNVGVIIFILTIATAFLGYCCV description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI2 16) chain N residue 173-204 type BINDING sequence NPTIQRFFALHYLVPFIIAAMVIMHLMALHIH description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI2 17) chain N residue 224-246 type BINDING sequence YFIFKDLVTVFLFMLILALFVFY description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI2 18) chain N residue 288-308 type BINDING sequence KLLGVITMFAAILVLLVLPFT description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI2 19) chain N residue 320-340 type BINDING sequence VLSKFFFFIFVFNFVLLGQIG description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI2 20) chain N residue 348-364 type BINDING sequence YVLMGQIATFIYFAYFL description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI2 21) chain N residue 28-51 type BINDING sequence YWWNMGSLLGLCLVIQIVTGIFMA description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB, ECO:0007744|PDB:3CXH source Swiss-Prot : SWS_FT_FI2 22) chain N residue 52-74 type BINDING sequence MHYSSNIELAFSSVEHIMRDVHN description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB source Swiss-Prot : SWS_FT_FI3 23) chain N residue 136-172 type BINDING sequence YGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVS description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB source Swiss-Prot : SWS_FT_FI3 24) chain N residue 247-287 type BINDING sequence SPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIP D description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB source Swiss-Prot : SWS_FT_FI3 25) chain N residue 341-347 type BINDING sequence ACHVEVP description axial binding residue => ECO:0000269|PubMed:1326054, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1YEA, ECO:0007744|PDB:1YEB source Swiss-Prot : SWS_FT_FI3

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