2JAE
The structure of L-amino acid oxidase from Rhodococcus opacus in the unbound state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001716 | molecular_function | L-amino-acid oxidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050025 | molecular_function | L-glutamate oxidase activity |
| A | 0050029 | molecular_function | L-lysine oxidase activity |
| A | 0106329 | molecular_function | L-phenylalaine oxidase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001716 | molecular_function | L-amino-acid oxidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050025 | molecular_function | L-glutamate oxidase activity |
| B | 0050029 | molecular_function | L-lysine oxidase activity |
| B | 0106329 | molecular_function | L-phenylalaine oxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD A1490 |
| Chain | Residue |
| A | GLY19 |
| A | ARG50 |
| A | ALA82 |
| A | THR83 |
| A | ARG84 |
| A | ALA259 |
| A | VAL261 |
| A | THR292 |
| A | ILE293 |
| A | TYR371 |
| A | TRP416 |
| A | GLY21 |
| A | TYR421 |
| A | ALA425 |
| A | GLY458 |
| A | ASP459 |
| A | ALA466 |
| A | TRP467 |
| A | GLN468 |
| A | ALA471 |
| A | HOH2034 |
| A | HOH2095 |
| A | PRO22 |
| A | HOH2320 |
| A | HOH2321 |
| A | HOH2346 |
| A | HOH2439 |
| A | HOH2488 |
| A | HOH2489 |
| A | ALA23 |
| A | LEU41 |
| A | GLU42 |
| A | ALA43 |
| A | ARG44 |
| A | GLY49 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD B1489 |
| Chain | Residue |
| B | GLY19 |
| B | GLY21 |
| B | PRO22 |
| B | ALA23 |
| B | LEU41 |
| B | GLU42 |
| B | ALA43 |
| B | ARG44 |
| B | GLY49 |
| B | ARG50 |
| B | ALA82 |
| B | THR83 |
| B | ARG84 |
| B | ALA259 |
| B | VAL261 |
| B | THR292 |
| B | ILE293 |
| B | SER321 |
| B | TYR371 |
| B | TRP416 |
| B | TYR421 |
| B | ALA425 |
| B | GLY458 |
| B | ASP459 |
| B | ALA466 |
| B | TRP467 |
| B | GLN468 |
| B | ALA471 |
| B | HOH2010 |
| B | HOH2041 |
| B | HOH2120 |
| B | HOH2335 |
| B | HOH2355 |
| B | HOH2502 |
| B | HOH2503 |
| B | HOH2504 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17234209, ECO:0007744|PDB:2JAE, ECO:0007744|PDB:2JB1, ECO:0007744|PDB:2JB2, ECO:0007744|PDB:2JB3 |
| Chain | Residue | Details |
| A | PRO22 | |
| B | ARG50 | |
| B | GLY81 | |
| B | VAL261 | |
| B | ASP459 | |
| A | GLU42 | |
| A | ARG50 | |
| A | GLY81 | |
| A | VAL261 | |
| A | ASP459 | |
| B | PRO22 | |
| B | GLU42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17234209, ECO:0007744|PDB:2JB1, ECO:0007744|PDB:2JB2 |
| Chain | Residue | Details |
| A | TYR371 | |
| A | ALA466 | |
| B | ARG84 | |
| B | GLN228 | |
| B | TYR371 | |
| B | ALA466 | |
| A | ARG84 | |
| A | GLN228 |
