5MXJ
Structure of the Y108F mutant of vanillyl alcohol oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005777 | cellular_component | peroxisome |
| A | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| A | 0015945 | biological_process | methanol metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018465 | molecular_function | vanillyl-alcohol oxidase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| A | 1903457 | biological_process | lactate catabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004458 | molecular_function | D-lactate dehydrogenase (cytochrome) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005777 | cellular_component | peroxisome |
| B | 0008720 | molecular_function | D-lactate dehydrogenase (NAD+) activity |
| B | 0015945 | biological_process | methanol metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018465 | molecular_function | vanillyl-alcohol oxidase activity |
| 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 | 26 |
| Details | binding site for residue FAD A 601 |
| Chain | Residue |
| A | TYR51 |
| A | ASP170 |
| A | LEU171 |
| A | GLY174 |
| A | SER175 |
| A | ASN179 |
| A | GLU182 |
| A | GLY184 |
| A | VAL185 |
| A | TYR187 |
| A | GLY260 |
| A | PRO99 |
| A | VAL262 |
| A | TRP413 |
| A | HIS422 |
| A | ARG504 |
| A | LYS545 |
| A | HOH701 |
| A | HOH723 |
| A | SER101 |
| A | ILE102 |
| A | GLY103 |
| A | ARG104 |
| A | ASN105 |
| A | SER106 |
| A | GLY110 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 602 |
| Chain | Residue |
| A | PRO189 |
| A | ARG300 |
| A | GLN306 |
| A | VAL308 |
| A | MET462 |
| A | HOH732 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| B | ASP493 |
| B | GLN512 |
| B | GLU515 |
| B | THR516 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 603 |
| Chain | Residue |
| B | LYS15 |
| B | ASN91 |
| B | LYS92 |
| B | ASN538 |
| B | HOH725 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for Di-peptide FAD B 601 and HIS B 422 |
| Chain | Residue |
| B | HIS61 |
| B | TRP98 |
| B | PRO99 |
| B | SER101 |
| B | ILE102 |
| B | GLY103 |
| B | ARG104 |
| B | ASN105 |
| B | SER106 |
| B | GLY107 |
| B | PRO169 |
| B | ASP170 |
| B | LEU171 |
| B | GLY174 |
| B | SER175 |
| B | ASN179 |
| B | GLU182 |
| B | GLY184 |
| B | VAL185 |
| B | TYR187 |
| B | GLY260 |
| B | ILE261 |
| B | VAL262 |
| B | TRP413 |
| B | ILE414 |
| B | ALA421 |
| B | LEU423 |
| B | PHE424 |
| B | ILE471 |
| B | ARG504 |
| B | LYS545 |
| B | HOH733 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 410 |
| Details | Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for the catalytic mechanism; Involved in substrate deprotonation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Tele-8alpha-FAD histidine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 103 |
| Chain | Residue | Details |
| A | PHE108 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP170 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS422 | activator, covalently attached, increase redox potential |
| A | TYR503 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG504 | activator, electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 103 |
| Chain | Residue | Details |
| B | PHE108 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP170 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS422 | activator, covalently attached, increase redox potential |
| B | TYR503 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG504 | activator, electrostatic stabiliser, hydrogen bond donor |
