1Q1W
Crystal Structure of Putidaredoxin Reductase from Pseudomonas putida
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| A | 0019383 | biological_process | (+)-camphor catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| B | 0019383 | biological_process | (+)-camphor catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD A 449 |
| Chain | Residue |
| A | GLY11 |
| A | LYS50 |
| A | THR81 |
| A | VAL83 |
| A | ALA109 |
| A | THR110 |
| A | GLY111 |
| A | ARG134 |
| A | ILE160 |
| A | GLY283 |
| A | ASP284 |
| A | GLY13 |
| A | GLU300 |
| A | SER301 |
| A | VAL302 |
| A | PRO303 |
| A | TRP330 |
| A | HOH455 |
| A | HOH456 |
| A | HOH462 |
| A | HOH477 |
| A | HOH494 |
| A | LEU14 |
| A | HOH511 |
| A | HOH524 |
| A | ALA15 |
| A | GLY36 |
| A | ASP37 |
| A | LEU45 |
| A | PRO46 |
| A | SER49 |
| site_id | AC2 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD B 450 |
| Chain | Residue |
| B | GLY11 |
| B | GLY13 |
| B | LEU14 |
| B | ALA15 |
| B | ASP37 |
| B | LEU45 |
| B | PRO46 |
| B | SER49 |
| B | LYS50 |
| B | THR81 |
| B | GLN82 |
| B | VAL83 |
| B | ALA109 |
| B | THR110 |
| B | GLY111 |
| B | GLY112 |
| B | LEU133 |
| B | ARG134 |
| B | LEU254 |
| B | GLY283 |
| B | ASP284 |
| B | GLU300 |
| B | SER301 |
| B | VAL302 |
| B | PRO303 |
| B | PHE329 |
| B | TRP330 |
| B | HOH455 |
| B | HOH459 |
| B | HOH464 |
| B | HOH466 |
| B | HOH480 |
| B | HOH483 |
| B | HOH514 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15095867, ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R, ECO:0007744|PDB:1Q1W, ECO:0007744|PDB:3LB8 |
| Chain | Residue | Details |
| A | ALA15 | |
| A | ASP37 | |
| A | LYS50 | |
| A | VAL83 | |
| B | ALA15 | |
| B | ASP37 | |
| B | LYS50 | |
| B | VAL83 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15095867, ECO:0000269|PubMed:20179327, ECO:0007744|PDB:1Q1R, ECO:0007744|PDB:3LB8 |
| Chain | Residue | Details |
| A | ARG134 | |
| A | ASP284 | |
| A | VAL302 | |
| B | ARG134 | |
| B | ASP284 | |
| B | VAL302 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY156 | |
| B | GLY156 |
