eF-site ID 1kyo-W PDB Code 1kyo Chain W 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 W:  TEFKAGSAKKGATLFKTRCLQCHTVEKGGPHKVGPNLHGI FGRHSGQAEGYSYTDANIKKNVLWDENNMSEYLTNPXKYI PGTKMAFGGLKKEKDRNDLITYLKKACE Description Functional site 1) chain W residue 18 type sequence R description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 2) chain W residue 19 type sequence C description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 3) chain W residue 22 type sequence C description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 4) chain W residue 23 type sequence H description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 5) chain W residue 33 type sequence V description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 6) chain W residue 34 type sequence G description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 7) chain W residue 40 type sequence I description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 8) chain W residue 45 type sequence S description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 9) chain W residue 46 type sequence G description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 10) chain W residue 51 type sequence Y description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 11) chain W residue 53 type sequence Y description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 12) chain W residue 54 type sequence T description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 13) chain W residue 57 type sequence N description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 14) chain W residue 64 type sequence W description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 15) chain W residue 72 type sequence Y description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 16) chain W residue 83 type sequence T description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 17) chain W residue 84 type sequence K description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 18) chain W residue 85 type sequence M description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 19) chain W residue 87 type sequence F description BINDING SITE FOR RESIDUE HEC W 526 source : BC2 20) chain W residue 20 type BINDING sequence L description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 21) chain W residue 23 type BINDING sequence H description covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 source Swiss-Prot : SWS_FT_FI1 22) chain W residue 24 type BINDING sequence T 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 23) chain W residue 86 type BINDING sequence A 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 24) chain W residue 78 type MOD_RES sequence K 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 25) chain W residue 79 type MOD_RES sequence Y description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 source Swiss-Prot : SWS_FT_FI4

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