2FYU
Crystal structure of bovine heart mitochondrial bc1 with jg144 inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004222 | molecular_function | metalloendopeptidase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0006508 | biological_process | proteolysis |
| B | 0045275 | cellular_component | respiratory chain complex III |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| C | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 0031966 | cellular_component | mitochondrial membrane |
| C | 0045275 | cellular_component | respiratory chain complex III |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048039 | molecular_function | ubiquinone binding |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| E | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| E | 0016020 | cellular_component | membrane |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| F | 0005743 | cellular_component | mitochondrial inner membrane |
| F | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| F | 0016020 | cellular_component | membrane |
| F | 0045275 | cellular_component | respiratory chain complex III |
| G | 0005739 | cellular_component | mitochondrion |
| G | 0005743 | cellular_component | mitochondrial inner membrane |
| G | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| G | 0016020 | cellular_component | membrane |
| G | 0021539 | biological_process | subthalamus development |
| G | 0021548 | biological_process | pons development |
| G | 0021680 | biological_process | cerebellar Purkinje cell layer development |
| G | 0021766 | biological_process | hippocampus development |
| G | 0021794 | biological_process | thalamus development |
| G | 0021854 | biological_process | hypothalamus development |
| G | 0021860 | biological_process | pyramidal neuron development |
| G | 0030901 | biological_process | midbrain development |
| G | 0045275 | cellular_component | respiratory chain complex III |
| H | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| I | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| J | 0005739 | cellular_component | mitochondrion |
| J | 0005743 | cellular_component | mitochondrial inner membrane |
| J | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| J | 0016020 | cellular_component | membrane |
| J | 0045275 | cellular_component | respiratory chain complex III |
| K | 0005739 | cellular_component | mitochondrion |
| K | 0005743 | cellular_component | mitochondrial inner membrane |
| K | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| K | 0045275 | cellular_component | respiratory chain complex III |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM C 381 |
| Chain | Residue |
| C | GLN44 |
| C | GLY130 |
| C | PRO134 |
| C | PHE179 |
| C | HIS182 |
| C | PHE183 |
| C | PRO186 |
| C | PHE187 |
| C | ILE45 |
| C | GLY48 |
| C | LEU51 |
| C | ARG80 |
| C | HIS83 |
| C | ALA87 |
| C | PHE90 |
| C | THR126 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM C 382 |
| Chain | Residue |
| C | TRP31 |
| C | GLY34 |
| C | LEU37 |
| C | HIS97 |
| C | VAL98 |
| C | ARG100 |
| C | SER106 |
| C | THR112 |
| C | TRP113 |
| C | GLY116 |
| C | VAL117 |
| C | LEU119 |
| C | HIS196 |
| C | LEU200 |
| C | SER205 |
| C | ASN206 |
| C | HOH1012 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FDN C 400 |
| Chain | Residue |
| C | MET124 |
| C | PHE128 |
| C | TYR131 |
| C | MET138 |
| C | GLY142 |
| C | ILE146 |
| C | LYS269 |
| C | PRO270 |
| C | GLU271 |
| C | TYR273 |
| C | PHE274 |
| C | TYR278 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HEM D 242 |
| Chain | Residue |
| D | VAL36 |
| D | CYS37 |
| D | CYS40 |
| D | HIS41 |
| D | ASN105 |
| D | PRO111 |
| D | ARG120 |
| D | TYR126 |
| D | PHE153 |
| D | GLY159 |
| D | MET160 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES E 200 |
| Chain | Residue |
| E | CYS139 |
| E | HIS141 |
| E | LEU142 |
| E | CYS158 |
| E | HIS161 |
| E | SER163 |
Functional Information from PROSITE/UniProt
| site_id | PS00143 |
| Number of Residues | 24 |
| Details | INSULINASE Insulinase family, zinc-binding region signature. GsryensnnlGtSHLLRLAsSlTT |
| Chain | Residue | Details |
| B | GLY54-THR77 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P31930","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CZ13","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CZ13","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q68FY0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DB77","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 161 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00968","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NU1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12269811","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16924113","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9204897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1L0N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NTZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NU1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4D6U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15312779","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16024040","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PP9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SQV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2A06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YBB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 329 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 144 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 81 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 101 |
| Details | Domain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 85 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9651245","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BE3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BGY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D855","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D855","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQ69","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P99028","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hr6 |
| Chain | Residue | Details |
| A | GLU60 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hr6 |
| Chain | Residue | Details |
| B | ARG70 |






