3Q9T
Crystal structure analysis of formate 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 | 41 |
| Details | BINDING SITE FOR RESIDUE FAY A 600 |
| Chain | Residue |
| A | GLY14 |
| A | GLY88 |
| A | LYS89 |
| A | THR90 |
| A | GLY93 |
| A | SER94 |
| A | SER95 |
| A | LEU97 |
| A | ASN98 |
| A | TYR99 |
| A | PHE100 |
| A | GLY16 |
| A | THR101 |
| A | VAL228 |
| A | HIS229 |
| A | SER230 |
| A | SER266 |
| A | GLN267 |
| A | GLY268 |
| A | GLU271 |
| A | PHE512 |
| A | ASP545 |
| A | THR17 |
| A | ALA546 |
| A | ARG556 |
| A | ILE557 |
| A | GLN558 |
| A | VAL561 |
| A | HOH589 |
| A | HOH594 |
| A | HOH595 |
| A | HOH603 |
| A | HOH608 |
| A | ALA18 |
| A | HOH749 |
| A | HOH784 |
| A | GLU38 |
| A | ALA39 |
| A | TRP66 |
| A | THR86 |
| A | ARG87 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD A 581 |
| Chain | Residue |
| A | TYR471 |
| A | PHE475 |
| A | HOH730 |
| A | HOH870 |
| A | HOH909 |
| B | LYS476 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MRD A 582 |
| Chain | Residue |
| A | ASP260 |
| A | HOH938 |
| C | ILE428 |
| C | ASN456 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A 1 |
| Chain | Residue |
| A | TYR68 |
| A | HIS229 |
| A | GLU271 |
| A | LYS274 |
| A | PRO441 |
| A | PHE442 |
| A | GLN445 |
| A | GLN446 |
| B | HOH775 |
| site_id | AC5 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAY B 600 |
| Chain | Residue |
| B | GLY14 |
| B | GLY16 |
| B | THR17 |
| B | ALA18 |
| B | GLU38 |
| B | ALA39 |
| B | TRP66 |
| B | THR86 |
| B | ARG87 |
| B | GLY88 |
| B | THR90 |
| B | GLY93 |
| B | SER94 |
| 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 | PHE512 |
| B | ASP545 |
| B | ALA546 |
| B | ARG556 |
| B | ILE557 |
| B | GLN558 |
| B | VAL561 |
| B | HOH587 |
| B | HOH591 |
| B | HOH623 |
| B | HOH642 |
| B | HOH654 |
| B | HOH671 |
| B | HOH735 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG B 1 |
| Chain | Residue |
| B | ARG206 |
| B | ASN344 |
| B | ARG345 |
| B | HOH901 |
| site_id | AC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAY C 600 |
| 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 | LEU97 |
| C | ASN98 |
| C | TYR99 |
| C | PHE100 |
| C | THR101 |
| C | VAL228 |
| C | HIS229 |
| C | SER230 |
| C | SER266 |
| C | GLN267 |
| C | GLY268 |
| C | GLU271 |
| C | PHE512 |
| C | ASP545 |
| C | ALA546 |
| C | ARG556 |
| C | ILE557 |
| C | GLN558 |
| C | HOH589 |
| C | HOH596 |
| C | HOH653 |
| C | HOH663 |
| C | HOH732 |
| C | HOH899 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD C 1 |
| Chain | Residue |
| C | TYR471 |
| C | PHE475 |
| C | GLU487 |
| C | LEU494 |
| C | HOH620 |
| C | HOH895 |
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 |
