1AHV
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH 2-NITRO-P-CRESOL
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 | 23 |
Details | BINDING SITE FOR RESIDUE FAD A 600 |
Chain | Residue |
A | ASP170 |
A | LEU171 |
A | SER175 |
A | ASN179 |
A | GLU182 |
A | GLY184 |
A | VAL185 |
A | TYR187 |
A | ILE261 |
A | VAL262 |
A | TRP413 |
A | HIS422 |
A | PHE424 |
A | ARG504 |
A | LYS545 |
A | NCR601 |
A | PRO99 |
A | SER101 |
A | ILE102 |
A | GLY103 |
A | ARG104 |
A | ASN105 |
A | PRO169 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NCR A 601 |
Chain | Residue |
A | TYR108 |
A | VAL185 |
A | TYR187 |
A | PHE424 |
A | THR459 |
A | ILE468 |
A | TYR503 |
A | FAD600 |
site_id | AC3 |
Number of Residues | 23 |
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 | ASP170 |
B | LEU171 |
B | SER175 |
B | ASN179 |
B | GLU182 |
B | GLY184 |
B | VAL185 |
B | TYR187 |
B | ILE261 |
B | VAL262 |
B | TRP413 |
B | HIS422 |
B | PHE424 |
B | ARG504 |
B | LYS545 |
B | NCR601 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NCR B 601 |
Chain | Residue |
B | TYR108 |
B | VAL185 |
B | TYR187 |
B | PHE424 |
B | THR459 |
B | ILE468 |
B | TYR503 |
B | FAD600 |
site_id | FAD |
Number of Residues | 2 |
Details | COFACTOR. |
Chain | Residue |
A | FAD600 |
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 | ASP170 | |
B | ASP170 |
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 | 5 |
Details | Annotated By Reference To The Literature 1vao |
Chain | Residue | Details |
A | ARG504 | |
A | HIS422 | |
A | TYR503 | |
A | ASP170 | |
A | TYR108 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1vao |
Chain | Residue | Details |
B | ARG504 | |
B | HIS422 | |
B | TYR503 | |
B | ASP170 | |
B | TYR108 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 103 |
Chain | Residue | Details |
A | TYR108 | 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 | TYR108 | 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 |