1Q1R
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 | 36 |
Details | BINDING SITE FOR RESIDUE FAD A 749 |
Chain | Residue |
A | GLY11 |
A | LYS50 |
A | THR81 |
A | VAL83 |
A | ALA109 |
A | THR110 |
A | GLY111 |
A | GLY112 |
A | ARG134 |
A | ILE160 |
A | LEU254 |
A | GLY13 |
A | GLY283 |
A | ASP284 |
A | GLU300 |
A | SER301 |
A | VAL302 |
A | PRO303 |
A | TRP330 |
A | HOH751 |
A | HOH757 |
A | HOH771 |
A | LEU14 |
A | HOH781 |
A | HOH794 |
A | HOH831 |
A | HOH832 |
A | HOH840 |
A | HOH869 |
A | HOH930 |
A | ALA15 |
A | GLY36 |
A | ASP37 |
A | LEU45 |
A | PRO46 |
A | SER49 |
site_id | AC2 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD B 750 |
Chain | Residue |
B | VAL10 |
B | GLY11 |
B | GLY13 |
B | LEU14 |
B | ALA15 |
B | GLY36 |
B | ASP37 |
B | LEU45 |
B | PRO46 |
B | SER49 |
B | LYS50 |
B | THR81 |
B | VAL83 |
B | ALA109 |
B | THR110 |
B | GLY111 |
B | GLY112 |
B | ARG134 |
B | ILE160 |
B | LEU254 |
B | GLY283 |
B | ASP284 |
B | GLU300 |
B | SER301 |
B | VAL302 |
B | PRO303 |
B | ALA305 |
B | TRP330 |
B | HOH752 |
B | HOH754 |
B | HOH756 |
B | HOH758 |
B | HOH777 |
B | HOH788 |
B | HOH829 |
B | HOH831 |
B | HOH865 |
B | HOH868 |
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 |