4N9Q
Crystal structure of paAzoR1 bound to ubiquinone-1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003960 | molecular_function | NADPH:quinone reductase activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0003960 | molecular_function | NADPH:quinone reductase activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN A 301 |
| Chain | Residue |
| A | SER10 |
| A | PHE100 |
| A | SER145 |
| A | GLY147 |
| A | GLY148 |
| A | PHE151 |
| A | GLU187 |
| A | HOH408 |
| A | HOH412 |
| B | VAL56 |
| B | PHE60 |
| A | ARG12 |
| A | SER16 |
| A | GLN17 |
| A | SER18 |
| A | PRO96 |
| A | MET97 |
| A | TYR98 |
| A | ASN99 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UQ1 A 302 |
| Chain | Residue |
| A | PHE60 |
| A | PHE120 |
| A | TYR131 |
| A | PHE173 |
| B | ASN99 |
| B | PHE100 |
| B | FMN301 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | LEU48 |
| A | ALA50 |
| A | SER104 |
| A | GLY105 |
| B | SER104 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | ARG30 |
| A | ARG40 |
| A | HOH429 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN B 301 |
| Chain | Residue |
| A | UQ1302 |
| B | SER10 |
| B | ARG12 |
| B | ARG15 |
| B | SER16 |
| B | GLN17 |
| B | SER18 |
| B | PRO96 |
| B | MET97 |
| B | TYR98 |
| B | ASN99 |
| B | PHE100 |
| B | SER145 |
| B | GLY147 |
| B | GLY148 |
| B | PHE151 |
| B | GLU187 |
| B | HOH406 |
| B | HOH413 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:17904577, ECO:0000269|PubMed:20057057, ECO:0000269|PubMed:20417637, ECO:0000269|PubMed:22355582, ECO:0000269|PubMed:24915188, ECO:0007744|PDB:2V9C, ECO:0007744|PDB:3KEG, ECO:0007744|PDB:3LT5, ECO:0007744|PDB:3R6W, ECO:0007744|PDB:4N65, ECO:0007744|PDB:4N9Q |
| Chain | Residue | Details |
| B | MET97 | |
| B | SER145 | |
| A | SER10 | |
| A | SER16 | |
| A | MET97 | |
| A | SER145 | |
| B | SER10 | |
| B | SER16 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:20417637, ECO:0000305|PubMed:22355582, ECO:0007744|PDB:3LT5, ECO:0007744|PDB:3R6W |
| Chain | Residue | Details |
| B | ASN99 | |
| B | TYR131 | |
| A | ASN99 | |
| A | TYR131 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20417637, ECO:0000269|PubMed:22355582, ECO:0000269|PubMed:24915188, ECO:0007744|PDB:3LT5, ECO:0007744|PDB:3R6W, ECO:0007744|PDB:4N65, ECO:0007744|PDB:4N9Q |
| Chain | Residue | Details |
| A | GLU187 | |
| B | GLU187 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:20057057, ECO:0000305|PubMed:20417637, ECO:0007744|PDB:3KEG, ECO:0007744|PDB:3LT5 |
| Chain | Residue | Details |
| A | GLU188 | |
| B | GLU188 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Important in the architecture of the active site => ECO:0000269|PubMed:20057057 |
| Chain | Residue | Details |
| A | TYR131 | |
| B | TYR131 |
