3H1I
Stigmatellin and antimycin bound cytochrome bc1 complex from chicken
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0045275 | cellular_component | respiratory chain complex III |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0045275 | cellular_component | respiratory chain complex III |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| C | 0006979 | biological_process | response to oxidative stress |
| 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 | 0045275 | cellular_component | respiratory chain complex III |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0005743 | cellular_component | mitochondrial inner membrane |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0045275 | cellular_component | respiratory chain complex III |
| 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 | 0045275 | cellular_component | respiratory chain complex III |
| G | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| 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 | 0005743 | cellular_component | mitochondrial inner membrane |
| J | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| J | 0009060 | biological_process | aerobic respiration |
| J | 0016020 | cellular_component | membrane |
| J | 0045275 | cellular_component | respiratory chain complex III |
| N | 0005743 | cellular_component | mitochondrial inner membrane |
| N | 0045275 | cellular_component | respiratory chain complex III |
| N | 0046872 | molecular_function | metal ion binding |
| O | 0005743 | cellular_component | mitochondrial inner membrane |
| O | 0045275 | cellular_component | respiratory chain complex III |
| O | 0046872 | molecular_function | metal ion binding |
| P | 0005737 | cellular_component | cytoplasm |
| P | 0005739 | cellular_component | mitochondrion |
| P | 0005743 | cellular_component | mitochondrial inner membrane |
| P | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| P | 0006979 | biological_process | response to oxidative stress |
| P | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| P | 0009055 | molecular_function | electron transfer activity |
| P | 0016020 | cellular_component | membrane |
| P | 0016491 | molecular_function | oxidoreductase activity |
| P | 0020037 | molecular_function | heme binding |
| P | 0022904 | biological_process | respiratory electron transport chain |
| P | 0045275 | cellular_component | respiratory chain complex III |
| P | 1902600 | biological_process | proton transmembrane transport |
| Q | 0005743 | cellular_component | mitochondrial inner membrane |
| Q | 0009055 | molecular_function | electron transfer activity |
| Q | 0020037 | molecular_function | heme binding |
| Q | 0045275 | cellular_component | respiratory chain complex III |
| R | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| R | 0016020 | cellular_component | membrane |
| R | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| S | 0005743 | cellular_component | mitochondrial inner membrane |
| S | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| S | 0045275 | cellular_component | respiratory chain complex III |
| T | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| T | 0045275 | cellular_component | respiratory chain complex III |
| U | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| V | 0008121 | molecular_function | quinol-cytochrome-c reductase activity |
| W | 0005743 | cellular_component | mitochondrial inner membrane |
| W | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| W | 0009060 | biological_process | aerobic respiration |
| W | 0016020 | cellular_component | membrane |
| W | 0045275 | cellular_component | respiratory chain complex III |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | GLN45 |
| C | LEU124 |
| C | THR127 |
| C | GLY131 |
| C | TYR132 |
| C | LEU134 |
| C | PRO135 |
| C | HIS183 |
| C | PHE184 |
| C | PRO187 |
| C | ILE46 |
| C | GLY49 |
| C | LEU52 |
| C | ALA53 |
| C | TYR56 |
| C | ARG81 |
| C | HIS84 |
| C | ALA85 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM C 502 |
| Chain | Residue |
| C | TRP32 |
| C | GLY35 |
| C | LEU38 |
| C | ALA39 |
| C | HIS98 |
| C | ARG101 |
| C | SER107 |
| C | THR113 |
| C | TRP114 |
| C | GLY117 |
| C | VAL118 |
| C | LEU120 |
| C | LEU121 |
| C | ILE190 |
| C | THR194 |
| C | HIS197 |
| C | LEU201 |
| C | SER206 |
| C | ASN207 |
| C | ANY2002 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC D 501 |
| Chain | Residue |
| D | VAL32 |
| D | VAL36 |
| D | CYS37 |
| D | CYS40 |
| D | HIS41 |
| D | ASN105 |
| D | ALA108 |
| D | PRO110 |
| D | ARG120 |
| D | TYR126 |
| D | PHE153 |
| D | GLY159 |
| D | MET160 |
| D | PRO163 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES E 501 |
| Chain | Residue |
| E | CYS139 |
| E | HIS141 |
| E | LEU142 |
| E | CYS144 |
| E | CYS158 |
| E | HIS161 |
| E | SER163 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM P 501 |
| Chain | Residue |
| P | GLN45 |
| P | ILE46 |
| P | GLY49 |
| P | LEU52 |
| P | ALA53 |
| P | ARG81 |
| P | HIS84 |
| P | ALA85 |
| P | LEU124 |
| P | THR127 |
| P | GLY131 |
| P | TYR132 |
| P | LEU134 |
| P | PRO135 |
| P | HIS183 |
| P | PHE184 |
| P | PRO187 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM P 502 |
| Chain | Residue |
| P | TRP32 |
| P | GLY35 |
| P | LEU38 |
| P | ALA39 |
| P | HIS98 |
| P | ARG101 |
| P | SER107 |
| P | THR113 |
| P | TRP114 |
| P | GLY117 |
| P | VAL118 |
| P | LEU120 |
| P | LEU121 |
| P | THR194 |
| P | HIS197 |
| P | LEU201 |
| P | ASN207 |
| P | ANY3002 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC Q 501 |
| Chain | Residue |
| Q | ASN105 |
| Q | ALA108 |
| Q | PRO110 |
| Q | ARG120 |
| Q | TYR126 |
| Q | PHE153 |
| Q | GLY159 |
| Q | MET160 |
| Q | PRO163 |
| Q | VAL32 |
| Q | VAL36 |
| Q | CYS37 |
| Q | CYS40 |
| Q | HIS41 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES R 501 |
| Chain | Residue |
| R | CYS139 |
| R | HIS141 |
| R | LEU142 |
| R | GLY143 |
| R | CYS144 |
| R | CYS158 |
| R | HIS161 |
| R | SER163 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SMA C 2001 |
| Chain | Residue |
| C | LEU122 |
| C | MET125 |
| C | ALA126 |
| C | PHE129 |
| C | GLY143 |
| C | VAL146 |
| C | ILE147 |
| C | PRO271 |
| C | GLU272 |
| C | PHE275 |
| C | TYR279 |
| R | HIS161 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ANY C 2002 |
| Chain | Residue |
| C | SER18 |
| C | LEU19 |
| C | ILE28 |
| C | TRP32 |
| C | SER36 |
| C | ALA39 |
| C | LEU42 |
| C | THR194 |
| C | ILE195 |
| C | LEU198 |
| C | PHE221 |
| C | TYR225 |
| C | ASP229 |
| C | HEM502 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDL D 2003 |
| Chain | Residue |
| C | ALA30 |
| C | ASN33 |
| C | LEU231 |
| C | GLY232 |
| C | MET236 |
| C | CDL2004 |
| D | TYR220 |
| D | LYS223 |
| D | ARG224 |
| F | HIS72 |
| F | ARG73 |
| G | ARG40 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CDL C 2004 |
| Chain | Residue |
| C | SER29 |
| C | ALA30 |
| C | TRP31 |
| C | PEE2007 |
| D | CDL2003 |
| G | ARG40 |
| G | PHE41 |
| G | GLN44 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEE E 2005 |
| Chain | Residue |
| A | PEE2008 |
| C | PHE227 |
| C | ILE230 |
| D | LYS226 |
| E | TYR37 |
| E | THR40 |
| E | THR47 |
| J | PHE14 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PEE C 2007 |
| Chain | Residue |
| C | TRP31 |
| C | PHE96 |
| C | ARG101 |
| C | TYR104 |
| C | TYR105 |
| C | PHE277 |
| C | THR317 |
| C | TRP327 |
| C | CDL2004 |
| F | TYR29 |
| G | GLN44 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEE A 2008 |
| Chain | Residue |
| A | TYR442 |
| C | HIS222 |
| E | PEE2005 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLC E 2009 |
| Chain | Residue |
| C | LEU79 |
| C | LEU241 |
| D | GLN200 |
| D | MET204 |
| D | LYS207 |
| D | MET208 |
| E | TYR49 |
| E | ALA50 |
| E | VAL54 |
| E | GLN57 |
| J | ASP36 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 2011 |
| Chain | Residue |
| C | PHE64 |
| C | ARG81 |
| C | ASN256 |
| C | PHE257 |
| D | TYR115 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNL P 2015 |
| Chain | Residue |
| P | THR199 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNL R 2103 |
| Chain | Residue |
| R | THR140 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNL C 2104 |
| Chain | Residue |
| C | ASN149 |
| site_id | CC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNL E 2105 |
| Chain | Residue |
| E | TYR178 |
| site_id | CC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SMA P 3001 |
| Chain | Residue |
| E | HIS161 |
| P | LEU122 |
| P | MET125 |
| P | ALA126 |
| P | PHE129 |
| P | GLY143 |
| P | VAL146 |
| P | ILE147 |
| P | LEU182 |
| P | LYS270 |
| P | PRO271 |
| P | GLU272 |
| P | PHE275 |
| P | TYR279 |
| site_id | CC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ANY P 3002 |
| Chain | Residue |
| P | LEU19 |
| P | ILE28 |
| P | TRP32 |
| P | SER36 |
| P | ALA39 |
| P | LEU42 |
| P | THR194 |
| P | ILE195 |
| P | LEU198 |
| P | PHE221 |
| P | TYR225 |
| P | ASP229 |
| P | HEM502 |
| site_id | CC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDL Q 3003 |
| Chain | Residue |
| P | ALA30 |
| P | ASN33 |
| P | LEU231 |
| P | GLY232 |
| P | MET236 |
| P | CDL3004 |
| Q | TYR220 |
| Q | LYS223 |
| Q | ARG224 |
| S | HIS72 |
| S | ARG73 |
| T | ARG40 |
| site_id | CC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CDL P 3004 |
| Chain | Residue |
| P | SER29 |
| P | ALA30 |
| P | TRP31 |
| P | PEE3007 |
| Q | CDL3003 |
| S | HIS72 |
| T | ARG40 |
| T | PHE41 |
| T | GLN44 |
| site_id | CC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEE P 3005 |
| Chain | Residue |
| P | PHE227 |
| P | ILE230 |
| Q | LYS226 |
| R | TYR37 |
| R | THR40 |
| R | THR47 |
| W | PHE14 |
| W | GLU32 |
| site_id | CC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PEE P 3007 |
| Chain | Residue |
| P | TRP31 |
| P | PHE96 |
| P | ARG101 |
| P | TYR104 |
| P | TYR105 |
| P | PHE277 |
| P | THR317 |
| P | TRP327 |
| P | LEU333 |
| P | CDL3004 |
| S | TYR29 |
| T | GLN44 |
| site_id | DC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEE N 3008 |
| Chain | Residue |
| N | TYR442 |
| P | HIS222 |
| site_id | DC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLC R 3009 |
| Chain | Residue |
| P | THR44 |
| P | TYR76 |
| P | LEU79 |
| Q | GLN200 |
| Q | MET204 |
| Q | LYS207 |
| R | TYR49 |
| R | ALA50 |
| R | VAL54 |
| R | GLN57 |
| site_id | DC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNL P 3010 |
| Chain | Residue |
| P | ALA85 |
| site_id | DC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL P 3011 |
| Chain | Residue |
| P | PHE64 |
| P | ARG81 |
| P | ASN256 |
| Q | TYR115 |
| site_id | DC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNL C 3015 |
| Chain | Residue |
| C | THR199 |
| C | HIS202 |
| site_id | DC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNL E 3103 |
| Chain | Residue |
| E | THR140 |
| site_id | DC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNL P 3104 |
| Chain | Residue |
| P | ASN149 |
| P | HIS159 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI3 |
| Number of Residues | 322 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"20025846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L70","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00968","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20025846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L72","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L74","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L75","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TGU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20025846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CWB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L72","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L74","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L75","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TGU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"20025846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L70","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L72","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L73","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L74","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L75","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3TGU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21575592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22690928","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BCC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CWB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L72","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 54 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P13272","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 66 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 266 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P13272","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 170 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9565029","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3H1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H1I","evidenceCode":"ECO:0007744"}]} |
| 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 |
| N | GLU60 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hr6 |
| Chain | Residue | Details |
| B | ARG70 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hr6 |
| Chain | Residue | Details |
| O | ARG70 |






