2JB1
The L-amino acid oxidase from Rhodococcus opacus in complex with L- alanine
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 | 8 |
Details | BINDING SITE FOR RESIDUE ALA A1490 |
Chain | Residue |
A | ARG84 |
A | GLN228 |
A | TYR371 |
A | ALA466 |
A | TRP467 |
A | FAD1489 |
A | HOH2546 |
A | HOH2549 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ALA B1490 |
Chain | Residue |
B | GLN228 |
B | TYR371 |
B | ALA466 |
B | TRP467 |
B | FAD1489 |
B | HOH2582 |
B | HOH2583 |
B | ARG84 |
site_id | AC3 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD A1489 |
Chain | Residue |
A | GLY19 |
A | GLY21 |
A | PRO22 |
A | ALA23 |
A | GLU42 |
A | ALA43 |
A | ARG44 |
A | GLY49 |
A | ARG50 |
A | GLY81 |
A | ALA82 |
A | THR83 |
A | ARG84 |
A | ALA259 |
A | VAL261 |
A | TYR371 |
A | TRP416 |
A | TYR421 |
A | ALA425 |
A | GLY458 |
A | ASP459 |
A | ALA466 |
A | TRP467 |
A | GLN468 |
A | ALA471 |
A | ALA1490 |
A | HOH2034 |
A | HOH2098 |
A | HOH2352 |
A | HOH2486 |
A | HOH2546 |
A | HOH2547 |
A | HOH2548 |
site_id | AC4 |
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 | GLY81 |
B | ALA82 |
B | THR83 |
B | ARG84 |
B | ALA259 |
B | VAL261 |
B | THR292 |
B | TYR371 |
B | TRP416 |
B | TYR421 |
B | ALA425 |
B | TRP426 |
B | GLY458 |
B | ASP459 |
B | ALA466 |
B | TRP467 |
B | GLN468 |
B | ALA471 |
B | ALA1490 |
B | HOH2043 |
B | HOH2125 |
B | HOH2379 |
B | HOH2579 |
B | HOH2580 |
B | HOH2581 |
B | HOH2583 |
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 |
B | ARG50 | |
B | GLY81 | |
B | VAL261 | |
B | ASP459 | |
A | PRO22 | |
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 |