6MO6
Crystal structure of the selenomethionine-substituted human sulfide:quinone oxidoreductase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0048038 | molecular_function | quinone binding |
| A | 0070221 | biological_process | sulfide oxidation, using sulfide:quinone oxidoreductase |
| A | 0070224 | molecular_function | sulfide:quinone oxidoreductase activity |
| A | 0071949 | molecular_function | FAD binding |
| A | 0106436 | molecular_function | glutathione-dependent sulfide quinone oxidoreductase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0048038 | molecular_function | quinone binding |
| B | 0070221 | biological_process | sulfide oxidation, using sulfide:quinone oxidoreductase |
| B | 0070224 | molecular_function | sulfide:quinone oxidoreductase activity |
| B | 0071949 | molecular_function | FAD binding |
| B | 0106436 | molecular_function | glutathione-dependent sulfide quinone oxidoreductase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0048038 | molecular_function | quinone binding |
| C | 0070221 | biological_process | sulfide oxidation, using sulfide:quinone oxidoreductase |
| C | 0070224 | molecular_function | sulfide:quinone oxidoreductase activity |
| C | 0071949 | molecular_function | FAD binding |
| C | 0106436 | molecular_function | glutathione-dependent sulfide quinone oxidoreductase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005743 | cellular_component | mitochondrial inner membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0048038 | molecular_function | quinone binding |
| D | 0070221 | biological_process | sulfide oxidation, using sulfide:quinone oxidoreductase |
| D | 0070224 | molecular_function | sulfide:quinone oxidoreductase activity |
| D | 0071949 | molecular_function | FAD binding |
| D | 0106436 | molecular_function | glutathione-dependent sulfide quinone oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | GLY52 |
| A | VAL118 |
| A | LEU145 |
| A | GLY146 |
| A | ASN169 |
| A | TYR170 |
| A | CYS201 |
| A | LYS207 |
| A | GLY335 |
| A | ASP336 |
| A | LYS344 |
| A | SER53 |
| A | THR345 |
| A | ALA346 |
| A | ALA347 |
| A | SER378 |
| A | PRO380 |
| A | LYS418 |
| A | HOH609 |
| A | HOH622 |
| A | HOH627 |
| A | GLY54 |
| A | VAL74 |
| A | GLU75 |
| A | PRO76 |
| A | GLN83 |
| A | PRO84 |
| A | ARG117 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | ARG61 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | GLY50 |
| B | GLY52 |
| B | SER53 |
| B | GLY54 |
| B | GLU75 |
| B | PRO76 |
| B | GLN83 |
| B | PRO84 |
| B | THR87 |
| B | ARG117 |
| B | VAL118 |
| B | LEU145 |
| B | GLY146 |
| B | ASN169 |
| B | TYR170 |
| B | CYS201 |
| B | LYS207 |
| B | GLY335 |
| B | ASP336 |
| B | LYS344 |
| B | THR345 |
| B | ALA346 |
| B | ALA347 |
| B | VAL349 |
| B | SER378 |
| B | CSS379 |
| B | PRO380 |
| B | LYS418 |
| B | HOH601 |
| B | HOH602 |
| B | HOH605 |
| B | HOH608 |
| B | HOH621 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | ARG61 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | GLY52 |
| C | SER53 |
| C | GLY54 |
| C | VAL74 |
| C | GLU75 |
| C | PRO76 |
| C | GLN83 |
| C | PRO84 |
| C | ARG117 |
| C | VAL118 |
| C | LEU145 |
| C | GLY146 |
| C | ASN169 |
| C | TYR170 |
| C | LYS200 |
| C | CYS201 |
| C | LYS207 |
| C | GLY335 |
| C | ASP336 |
| C | LYS344 |
| C | THR345 |
| C | ALA346 |
| C | ALA347 |
| C | VAL349 |
| C | SER378 |
| C | CSS379 |
| C | PRO380 |
| C | LYS418 |
| C | HOH611 |
| C | HOH623 |
| C | HOH627 |
| C | HOH632 |
| C | HOH640 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 502 |
| Chain | Residue |
| C | ARG61 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| D | GLY54 |
| D | VAL74 |
| D | GLU75 |
| D | PRO76 |
| D | GLN83 |
| D | PRO84 |
| D | ARG117 |
| D | VAL118 |
| D | ALA144 |
| D | LEU145 |
| D | GLY146 |
| D | ASN169 |
| D | TYR170 |
| D | CYS201 |
| D | LYS207 |
| D | GLY335 |
| D | ASP336 |
| D | LYS344 |
| D | THR345 |
| D | ALA346 |
| D | ALA347 |
| D | SER378 |
| D | PRO380 |
| D | LYS418 |
| D | HOH602 |
| D | HOH606 |
| D | HOH626 |
| D | HOH641 |
| D | GLY52 |
| D | SER53 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 502 |
| Chain | Residue |
| D | ARG61 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Cysteine persulfide intermediate => ECO:0000269|PubMed:30905673, ECO:0000303|PubMed:22852582 |
| Chain | Residue | Details |
| A | CYS201 | |
| A | CSS379 | |
| B | CYS201 | |
| B | CSS379 | |
| C | CYS201 | |
| C | CSS379 | |
| D | CYS201 | |
| D | CSS379 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30905673 |
| Chain | Residue | Details |
| A | SER53 | |
| B | VAL118 | |
| B | ASP336 | |
| B | LYS344 | |
| C | SER53 | |
| C | GLU75 | |
| C | GLN83 | |
| C | VAL118 | |
| C | ASP336 | |
| C | LYS344 | |
| D | SER53 | |
| A | GLU75 | |
| D | GLU75 | |
| D | GLN83 | |
| D | VAL118 | |
| D | ASP336 | |
| D | LYS344 | |
| A | GLN83 | |
| A | VAL118 | |
| A | ASP336 | |
| A | LYS344 | |
| B | SER53 | |
| B | GLU75 | |
| B | GLN83 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9R112 |
| Chain | Residue | Details |
| A | LYS173 | |
| B | LYS173 | |
| C | LYS173 | |
| D | LYS173 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9R112 |
| Chain | Residue | Details |
| A | SER343 | |
| B | SER343 | |
| C | SER343 | |
| D | SER343 |
