1E0Y
Structure of the D170S/T457E double 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 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 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 | 21 |
| Details | BINDING SITE FOR RESIDUE FAD A 600 |
| Chain | Residue |
| A | SER101 |
| A | ASN179 |
| A | GLU182 |
| A | GLY184 |
| A | VAL185 |
| A | TYR187 |
| A | GLY260 |
| A | VAL262 |
| A | TRP413 |
| A | ILE414 |
| A | HIS422 |
| A | ILE102 |
| A | ARG504 |
| A | LYS545 |
| A | GLY103 |
| A | ARG104 |
| A | ASN105 |
| A | PRO169 |
| A | SER170 |
| A | GLY174 |
| A | SER175 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD B 600 |
| Chain | Residue |
| B | PRO99 |
| B | SER101 |
| B | ILE102 |
| B | GLY103 |
| B | ARG104 |
| B | ASN105 |
| B | PRO169 |
| B | SER170 |
| B | GLY174 |
| B | SER175 |
| B | ASN179 |
| B | GLU182 |
| B | GLY184 |
| B | VAL185 |
| B | TYR187 |
| B | GLY260 |
| B | VAL262 |
| B | TRP413 |
| B | ILE414 |
| B | HIS422 |
| B | PHE424 |
| B | ARG504 |
| B | LYS545 |
| B | FCR601 |
| B | HOH2038 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FCR B 601 |
| Chain | Residue |
| B | TYR108 |
| B | SER170 |
| B | TYR187 |
| B | PHE424 |
| B | GLU457 |
| B | ILE468 |
| B | TYR503 |
| B | ARG504 |
| B | FAD600 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | TYR108 | |
| A | TYR503 | |
| A | ARG504 | |
| B | TYR108 | |
| B | TYR503 | |
| B | ARG504 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Important for the catalytic mechanism; Involved in substrate deprotonation |
| Chain | Residue | Details |
| A | SER170 | |
| B | SER170 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Tele-8alpha-FAD histidine |
| Chain | Residue | Details |
| A | HIS422 | |
| B | HIS422 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dii |
| Chain | Residue | Details |
| A | ARG504 | |
| A | HIS466 | |
| A | GLU410 | |
| A | TYR503 | |
| A | GLU457 | |
| A | TYR108 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1dii |
| Chain | Residue | Details |
| B | ARG504 | |
| B | HIS466 | |
| B | GLU410 | |
| B | TYR503 | |
| B | GLU457 | |
| B | TYR108 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1dii |
| Chain | Residue | Details |
| A | ARG504 | |
| A | HIS422 | |
| A | TYR503 | |
| A | SER170 | |
| A | TYR108 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1dii |
| Chain | Residue | Details |
| B | ARG504 | |
| B | HIS422 | |
| B | TYR503 | |
| B | SER170 | |
| B | TYR108 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 103 |
| Chain | Residue | Details |
| A | TYR108 | electrostatic stabiliser, hydrogen bond donor |
| A | SER170 | 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 | TYR108 | electrostatic stabiliser, hydrogen bond donor |
| B | SER170 | 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 |
