5YB8
L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 - L-arginine complex
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 | 0004497 | molecular_function | monooxygenase activity |
A | 0009063 | biological_process | amino acid catabolic process |
A | 0009851 | biological_process | auxin biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0001716 | molecular_function | L-amino-acid oxidase activity |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0009063 | biological_process | amino acid catabolic process |
B | 0009851 | biological_process | auxin biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0001716 | molecular_function | L-amino-acid oxidase activity |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0009063 | biological_process | amino acid catabolic process |
C | 0009851 | biological_process | auxin biosynthetic process |
C | 0016491 | molecular_function | oxidoreductase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0001716 | molecular_function | L-amino-acid oxidase activity |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0009063 | biological_process | amino acid catabolic process |
D | 0009851 | biological_process | auxin biosynthetic process |
D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue ARG A 601 |
Chain | Residue |
A | ARG102 |
A | ASP238 |
A | TYR416 |
A | TRP418 |
A | ALA515 |
A | TRP516 |
A | FAD604 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue ARG A 602 |
Chain | Residue |
A | ARG394 |
A | LEU395 |
D | THR337 |
D | GLU344 |
D | GLN349 |
D | TRP352 |
D | ASP356 |
A | GLY141 |
A | ASP393 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ARG A 603 |
Chain | Residue |
A | GLU344 |
A | GLN349 |
A | ASP356 |
D | ARG394 |
D | LEU395 |
site_id | AC4 |
Number of Residues | 37 |
Details | binding site for residue FAD A 604 |
Chain | Residue |
A | VAL51 |
A | GLY52 |
A | GLY54 |
A | ILE55 |
A | ALA56 |
A | GLU75 |
A | ALA76 |
A | SER77 |
A | LYS78 |
A | GLY81 |
A | ARG82 |
A | LEU83 |
A | GLY99 |
A | GLY100 |
A | MET101 |
A | ARG102 |
A | PHE103 |
A | GLY300 |
A | VAL301 |
A | CYS331 |
A | LEU335 |
A | ILE340 |
A | SER363 |
A | TRP463 |
A | PHE469 |
A | ALA472 |
A | PHE473 |
A | GLY507 |
A | ASP508 |
A | ALA515 |
A | TRP516 |
A | VAL517 |
A | ARG601 |
A | HOH711 |
A | HOH730 |
A | HOH746 |
A | HOH758 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue ARG B 601 |
Chain | Residue |
B | ARG102 |
B | ASP238 |
B | TYR416 |
B | TRP418 |
B | ALA515 |
B | TRP516 |
B | FAD603 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue ARG B 602 |
Chain | Residue |
B | GLY141 |
B | ASP393 |
B | ARG394 |
B | LEU395 |
B | HOH704 |
C | THR337 |
C | GLU344 |
C | GLN349 |
C | TRP352 |
C | ASP356 |
site_id | AC7 |
Number of Residues | 40 |
Details | binding site for residue FAD B 603 |
Chain | Residue |
B | TYR416 |
B | TRP463 |
B | PHE469 |
B | ALA472 |
B | PHE473 |
B | GLY507 |
B | ASP508 |
B | ALA515 |
B | TRP516 |
B | VAL517 |
B | ALA520 |
B | ARG601 |
B | HOH705 |
B | HOH732 |
B | HOH750 |
B | HOH783 |
B | VAL51 |
B | GLY52 |
B | GLY54 |
B | ILE55 |
B | ALA56 |
B | TYR74 |
B | GLU75 |
B | ALA76 |
B | SER77 |
B | LYS78 |
B | GLY81 |
B | ARG82 |
B | LEU83 |
B | GLY99 |
B | GLY100 |
B | MET101 |
B | ARG102 |
B | PHE103 |
B | GLY300 |
B | VAL301 |
B | CYS331 |
B | LEU335 |
B | ILE340 |
B | SER363 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue ARG C 601 |
Chain | Residue |
C | ARG102 |
C | ASP238 |
C | TYR416 |
C | ALA515 |
C | TRP516 |
C | FAD603 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue ARG C 602 |
Chain | Residue |
B | THR337 |
B | GLU344 |
B | GLN349 |
B | ASP356 |
C | ARG394 |
C | LEU395 |
site_id | AD1 |
Number of Residues | 35 |
Details | binding site for residue FAD C 603 |
Chain | Residue |
C | VAL51 |
C | GLY52 |
C | GLY54 |
C | ILE55 |
C | ALA56 |
C | TYR74 |
C | GLU75 |
C | ALA76 |
C | LYS78 |
C | GLY81 |
C | ARG82 |
C | LEU83 |
C | GLY99 |
C | GLY100 |
C | MET101 |
C | ARG102 |
C | PHE103 |
C | VAL301 |
C | THR330 |
C | CYS331 |
C | LEU335 |
C | SER363 |
C | TYR416 |
C | PHE469 |
C | ALA472 |
C | PHE473 |
C | GLY507 |
C | ASP508 |
C | ALA515 |
C | TRP516 |
C | VAL517 |
C | ALA520 |
C | ARG601 |
C | HOH712 |
C | HOH733 |
site_id | AD2 |
Number of Residues | 10 |
Details | binding site for residue ARG D 601 |
Chain | Residue |
D | ARG102 |
D | ASP238 |
D | ASN241 |
D | MET361 |
D | TYR416 |
D | TRP418 |
D | PHE473 |
D | ALA515 |
D | TRP516 |
D | FAD602 |
site_id | AD3 |
Number of Residues | 38 |
Details | binding site for residue FAD D 602 |
Chain | Residue |
D | VAL51 |
D | GLY52 |
D | GLY54 |
D | ILE55 |
D | ALA56 |
D | TYR74 |
D | GLU75 |
D | ALA76 |
D | GLY80 |
D | GLY81 |
D | ARG82 |
D | LEU83 |
D | GLY99 |
D | GLY100 |
D | MET101 |
D | ARG102 |
D | PHE103 |
D | GLY300 |
D | VAL301 |
D | THR330 |
D | CYS331 |
D | LEU335 |
D | ILE340 |
D | SER363 |
D | TYR416 |
D | PHE469 |
D | ALA472 |
D | PHE473 |
D | GLY507 |
D | ASP508 |
D | ALA515 |
D | TRP516 |
D | VAL517 |
D | ALA520 |
D | ARG601 |
D | HOH712 |
D | HOH715 |
D | HOH742 |