5FXF
Crystal structure of eugenol oxidase in complex with benzoate
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 | 33 |
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 | GLU378 |
A | HIS390 |
A | ARG472 |
A | LYS513 |
A | BEZ601 |
A | HOH2036 |
A | HOH2041 |
A | SER84 |
A | HOH2075 |
A | HOH2078 |
A | HOH2187 |
A | HOH2190 |
A | THR85 |
A | GLY86 |
A | LYS87 |
A | ASN88 |
A | ASN89 |
A | THR106 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BEZ A 601 |
Chain | Residue |
A | TYR91 |
A | VAL166 |
A | GLN425 |
A | ILE427 |
A | TYR471 |
A | ARG472 |
A | FAD600 |
site_id | AC3 |
Number of Residues | 31 |
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 | LEU162 |
B | GLY165 |
B | VAL166 |
B | TYR168 |
B | GLY225 |
B | ILE226 |
B | VAL227 |
B | HIS390 |
B | ARG472 |
B | LYS513 |
B | BEZ601 |
B | HOH2016 |
B | HOH2018 |
B | HOH2110 |
B | HOH2113 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BEZ B 601 |
Chain | Residue |
B | TYR91 |
B | VAL166 |
B | ILE427 |
B | LEU438 |
B | TYR471 |
B | ARG472 |
B | FAD600 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 1527 |
Chain | Residue |
B | PHE175 |
B | MET176 |
B | GLN178 |
B | PRO208 |
B | PHE214 |
B | ASP216 |
B | HOH2054 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 1527 |
Chain | Residue |
A | PHE175 |
A | MET176 |
A | GLN178 |
A | PRO208 |
A | PHE214 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 1528 |
Chain | Residue |
A | ARG402 |
A | HOH2120 |
B | LYS119 |
B | GLU255 |
B | ARG402 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1528 |
Chain | Residue |
A | GLY429 |
A | GLU432 |
A | HIS434 |
A | VAL166 |
A | GLY167 |
A | GLY172 |
A | ILE427 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 1529 |
Chain | Residue |
B | ASP479 |
B | TRP517 |
B | PHE521 |
B | ARG522 |
B | GLY523 |
B | GLN524 |
B | LEU526 |