eF-site ID 1kb9-D PDB Code 1kb9 Chain D click to enlarge Title YEAST CYTOCHROME BC1 COMPLEX Classification OXIDOREDUCTASE/ELECTRON TRANSPORT Compound UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I Source null (1KB9) Sequence D:  MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVC AACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQ GNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGG SIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEP EHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV FNPPKP 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 D residue 100 type sequence V description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 2) chain D residue 101 type sequence C description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 3) chain D residue 104 type sequence C description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 4) chain D residue 105 type sequence H description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 5) chain D residue 169 type sequence N description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 6) chain D residue 175 type sequence P description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 7) chain D residue 184 type sequence R description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 8) chain D residue 190 type sequence Y description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 9) chain D residue 191 type sequence I description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 10) chain D residue 218 type sequence F description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 11) chain D residue 223 type sequence I description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 12) chain D residue 224 type sequence A description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 13) chain D residue 225 type sequence M description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 14) chain D residue 228 type sequence V description BINDING SITE FOR RESIDUE HEM D 503 source : AC3 15) chain D residue 269 type sequence L description BINDING SITE FOR RESIDUE PIE C 508 source : AC7 16) chain D residue 272 type sequence K description BINDING SITE FOR RESIDUE PIE C 508 source : AC7 17) chain D residue 273 type sequence T description BINDING SITE FOR RESIDUE PIE C 508 source : AC7 18) chain D residue 276 type sequence I description BINDING SITE FOR RESIDUE PIE C 508 source : AC7 19) chain D residue 281 type sequence Y description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 20) chain D residue 288 type sequence K description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 21) chain D residue 289 type sequence K description BINDING SITE FOR RESIDUE CDL C 511 source : AC9 22) chain D residue 104 type TOPO_DOM sequence C description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 source Swiss-Prot : SWS_FT_FI3 23) chain D residue 225 type BINDING sequence M 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

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