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 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 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 |
A | SER10 | |
A | SER16 | |
A | MET97 | |
A | SER145 | |
B | SER10 | |
B | SER16 | |
B | MET97 | |
B | SER145 |
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 |
A | ASN99 | |
A | TYR131 | |
B | ASN99 | |
B | 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 |