5FXP
Crystal structure of eugenol oxidase in complex with vanillin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
A | 0008720 | molecular_function | D-lactate dehydrogenase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0018465 | molecular_function | vanillyl-alcohol oxidase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0071949 | molecular_function | FAD binding |
A | 1903457 | biological_process | lactate catabolic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
B | 0008720 | molecular_function | D-lactate dehydrogenase activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018465 | molecular_function | vanillyl-alcohol oxidase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0071949 | molecular_function | FAD binding |
B | 1903457 | biological_process | lactate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD A 600 |
Chain | Residue |
A | PRO82 |
A | PRO150 |
A | ASP151 |
A | GLY155 |
A | SER156 |
A | GLY159 |
A | ASN160 |
A | LEU162 |
A | GLY165 |
A | VAL166 |
A | TYR168 |
A | VAL83 |
A | GLY225 |
A | ILE226 |
A | VAL227 |
A | LEU381 |
A | HIS390 |
A | ARG472 |
A | LYS513 |
A | V55601 |
A | SER84 |
A | THR85 |
A | GLY86 |
A | LYS87 |
A | ASN88 |
A | ASN89 |
A | THR106 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE V55 A 601 |
Chain | Residue |
A | TYR91 |
A | ASP151 |
A | TYR168 |
A | GLN425 |
A | ILE427 |
A | VAL436 |
A | LEU438 |
A | TYR471 |
A | ARG472 |
A | FAD600 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE FAD B 600 |
Chain | Residue |
B | PRO82 |
B | VAL83 |
B | SER84 |
B | THR85 |
B | GLY86 |
B | LYS87 |
B | ASN88 |
B | ASN89 |
B | THR106 |
B | PRO150 |
B | ASP151 |
B | LEU152 |
B | GLY155 |
B | SER156 |
B | GLY159 |
B | ASN160 |
B | ASP163 |
B | GLY165 |
B | VAL166 |
B | TYR168 |
B | GLY225 |
B | ILE226 |
B | VAL227 |
B | LEU381 |
B | HIS390 |
B | ARG472 |
B | LYS513 |
B | V55601 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE V55 B 601 |
Chain | Residue |
B | TYR91 |
B | ASP151 |
B | GLN425 |
B | VAL436 |
B | TYR471 |
B | ARG472 |
B | FAD600 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 1527 |
Chain | Residue |
A | ASP479 |
A | TRP517 |
A | GLY523 |
A | ASN525 |