3W54
Crystal structure of cyanide-insensitive alternative oxidase from Trypanosoma brucei with colletochlorin B
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0009916 | molecular_function | alternative oxidase activity |
| A | 0010230 | biological_process | alternative respiration |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0008199 | molecular_function | ferric iron binding |
| B | 0009916 | molecular_function | alternative oxidase activity |
| B | 0010230 | biological_process | alternative respiration |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0008199 | molecular_function | ferric iron binding |
| C | 0009916 | molecular_function | alternative oxidase activity |
| C | 0010230 | biological_process | alternative respiration |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0022904 | biological_process | respiratory electron transport chain |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005743 | cellular_component | mitochondrial inner membrane |
| D | 0008199 | molecular_function | ferric iron binding |
| D | 0009916 | molecular_function | alternative oxidase activity |
| D | 0010230 | biological_process | alternative respiration |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0022904 | biological_process | respiratory electron transport chain |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 501 |
| Chain | Residue |
| A | GLU123 |
| A | GLU162 |
| A | HIS165 |
| A | GLU266 |
| A | FE502 |
| A | OH503 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE A 502 |
| Chain | Residue |
| A | FE501 |
| A | OH503 |
| A | HOH643 |
| A | GLU162 |
| A | GLU213 |
| A | GLU266 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OH A 503 |
| Chain | Residue |
| A | GLU123 |
| A | GLU162 |
| A | GLU213 |
| A | GLU266 |
| A | FE501 |
| A | FE502 |
| A | RNB504 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE RNB A 504 |
| Chain | Residue |
| A | CYS95 |
| A | ARG118 |
| A | LEU122 |
| A | MET190 |
| A | LEU212 |
| A | GLU215 |
| A | ALA216 |
| A | THR219 |
| A | OH503 |
| A | HOH643 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | ARG173 |
| A | PRO175 |
| A | GLY176 |
| A | LEU179 |
| A | HOH661 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 501 |
| Chain | Residue |
| B | GLU123 |
| B | GLU162 |
| B | HIS165 |
| B | GLU266 |
| B | FE502 |
| B | OH503 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 502 |
| Chain | Residue |
| B | GLU162 |
| B | GLU213 |
| B | GLU266 |
| B | FE501 |
| B | OH503 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OH B 503 |
| Chain | Residue |
| B | GLU123 |
| B | ALA126 |
| B | GLU162 |
| B | GLU266 |
| B | FE501 |
| B | FE502 |
| B | RNB504 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RNB B 504 |
| Chain | Residue |
| B | ARG96 |
| B | ARG118 |
| B | CYS119 |
| B | LEU122 |
| B | LEU212 |
| B | GLU215 |
| B | ALA216 |
| B | THR219 |
| B | OH503 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 501 |
| Chain | Residue |
| C | GLU123 |
| C | GLU162 |
| C | HIS165 |
| C | GLU266 |
| C | FE502 |
| C | OH503 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE C 502 |
| Chain | Residue |
| C | GLU162 |
| C | GLU213 |
| C | GLU266 |
| C | FE501 |
| C | OH503 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OH C 503 |
| Chain | Residue |
| C | GLU123 |
| C | ALA126 |
| C | GLU162 |
| C | GLU266 |
| C | FE501 |
| C | FE502 |
| C | RNB504 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE RNB C 504 |
| Chain | Residue |
| C | ARG118 |
| C | CYS119 |
| C | LEU122 |
| C | GLU123 |
| C | LEU212 |
| C | ALA216 |
| C | THR219 |
| C | TYR220 |
| C | OH503 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE D 501 |
| Chain | Residue |
| D | GLU123 |
| D | GLU162 |
| D | HIS165 |
| D | GLU266 |
| D | FE502 |
| D | OH503 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 502 |
| Chain | Residue |
| D | GLU162 |
| D | GLU213 |
| D | GLU266 |
| D | FE501 |
| D | OH503 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OH D 503 |
| Chain | Residue |
| D | GLU123 |
| D | ALA126 |
| D | GLU162 |
| D | GLU266 |
| D | FE501 |
| D | FE502 |
| D | RNB504 |
| site_id | BC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE RNB D 504 |
| Chain | Residue |
| D | ARG96 |
| D | ARG118 |
| D | CYS119 |
| D | LEU122 |
| D | GLU123 |
| D | LEU212 |
| D | GLU215 |
| D | ALA216 |
| D | THR219 |
| D | OH503 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 505 |
| Chain | Residue |
| D | SER117 |
| D | ARG173 |
| D | PRO175 |
| D | GLY176 |
| D | LEU179 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 506 |
| Chain | Residue |
| D | ARG137 |
| D | ASN286 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23487766","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3W54","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
