5ZU3
Effect of mutation (R554K) on FAD modification in Aspergillus oryzae RIB40formate oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0008812 | molecular_function | choline dehydrogenase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0008812 | molecular_function | choline dehydrogenase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0008812 | molecular_function | choline dehydrogenase activity |
| C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| C | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 39 |
| Details | binding site for residue FAY A 601 |
| Chain | Residue |
| A | GLY14 |
| A | GLY88 |
| A | THR90 |
| A | GLY93 |
| A | SER94 |
| A | SER95 |
| A | LEU97 |
| A | ASN98 |
| A | TYR99 |
| A | PHE100 |
| A | THR101 |
| A | GLY16 |
| A | VAL228 |
| A | HIS229 |
| A | SER230 |
| A | SER266 |
| A | GLN267 |
| A | GLY268 |
| A | GLU271 |
| A | PHE510 |
| A | ASP543 |
| A | ALA544 |
| A | THR17 |
| A | LYS554 |
| A | ILE555 |
| A | GLN556 |
| A | VAL559 |
| A | HOH748 |
| A | HOH775 |
| A | HOH797 |
| A | HOH809 |
| A | HOH854 |
| A | HOH891 |
| A | ALA18 |
| A | GLU38 |
| A | ALA39 |
| A | TRP66 |
| A | THR86 |
| A | ARG87 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MPD A 602 |
| Chain | Residue |
| A | TYR469 |
| A | PHE473 |
| A | LEU492 |
| A | HOH773 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue MPD A 603 |
| Chain | Residue |
| A | ASP260 |
| C | PRO384 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MPD A 604 |
| Chain | Residue |
| A | ASP440 |
| A | PRO441 |
| A | PHE442 |
| B | GLU254 |
| B | ASP440 |
| B | PRO441 |
| B | PHE442 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue ACT A 605 |
| Chain | Residue |
| A | TYR68 |
| A | HIS229 |
| A | GLU271 |
| A | LYS274 |
| A | PRO441 |
| A | PHE442 |
| A | GLN443 |
| A | GLN444 |
| site_id | AC6 |
| Number of Residues | 40 |
| Details | binding site for residue FAY B 601 |
| Chain | Residue |
| B | HOH822 |
| B | GLY14 |
| B | GLY16 |
| B | THR17 |
| B | ALA18 |
| B | GLU38 |
| B | ALA39 |
| B | TRP66 |
| B | THR86 |
| B | ARG87 |
| B | GLY88 |
| B | LYS89 |
| B | THR90 |
| B | GLY93 |
| B | SER94 |
| B | SER95 |
| B | LEU97 |
| B | ASN98 |
| B | TYR99 |
| B | PHE100 |
| B | THR101 |
| B | VAL228 |
| B | HIS229 |
| B | SER230 |
| B | SER266 |
| B | GLN267 |
| B | GLY268 |
| B | GLU271 |
| B | PHE510 |
| B | ASP543 |
| B | ALA544 |
| B | LYS554 |
| B | ILE555 |
| B | GLN556 |
| B | VAL559 |
| B | HOH714 |
| B | HOH726 |
| B | HOH742 |
| B | HOH786 |
| B | HOH797 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MPD B 602 |
| Chain | Residue |
| B | GLU162 |
| B | ARG206 |
| B | ARG345 |
| B | SER346 |
| site_id | AC8 |
| Number of Residues | 37 |
| Details | binding site for residue FAY C 601 |
| Chain | Residue |
| C | GLY14 |
| C | GLY16 |
| C | THR17 |
| C | ALA18 |
| C | GLU38 |
| C | ALA39 |
| C | TRP66 |
| C | THR86 |
| C | ARG87 |
| C | GLY88 |
| C | THR90 |
| C | GLY93 |
| C | SER94 |
| C | SER95 |
| C | LEU97 |
| C | ASN98 |
| C | TYR99 |
| C | PHE100 |
| C | THR101 |
| C | VAL228 |
| C | SER230 |
| C | SER266 |
| C | GLN267 |
| C | GLY268 |
| C | GLU271 |
| C | PHE510 |
| C | ASP543 |
| C | ALA544 |
| C | LYS554 |
| C | ILE555 |
| C | GLN556 |
| C | VAL559 |
| C | HOH744 |
| C | HOH776 |
| C | HOH783 |
| C | HOH793 |
| C | HOH798 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MPD C 602 |
| Chain | Residue |
| C | TYR469 |
| C | PHE473 |
| C | LEU492 |
| C | HOH710 |
| C | HOH713 |
Functional Information from PROSITE/UniProt
| site_id | PS00623 |
| Number of Residues | 24 |
| Details | GMC_OXRED_1 GMC oxidoreductases signature 1. GKtLGGSSsLNyftWvpGhkatfD |
| Chain | Residue | Details |
| A | GLY88-ASP111 |
