5Y9D
Crystal structure of acyl-coA oxidase1 from Yarrowia lipolytica
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003997 | molecular_function | acyl-CoA oxidase activity |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005777 | cellular_component | peroxisome |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0003997 | molecular_function | acyl-CoA oxidase activity |
| B | 0005504 | molecular_function | fatty acid binding |
| B | 0005777 | cellular_component | peroxisome |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | binding site for residue FAD A 701 |
| Chain | Residue |
| A | PHE146 |
| A | VAL439 |
| A | THR442 |
| A | TRP443 |
| A | GLU444 |
| A | ASP446 |
| B | ARG317 |
| B | GLN319 |
| B | PHE320 |
| B | ILE331 |
| B | TYR334 |
| A | MET148 |
| B | ARG340 |
| B | GLN417 |
| B | ALA418 |
| B | GLY420 |
| B | GLY421 |
| B | TYR424 |
| B | HOH809 |
| A | THR149 |
| A | HIS153 |
| A | GLY154 |
| A | SER155 |
| A | TRP186 |
| A | GLY188 |
| A | ASN247 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | binding site for residue FAD B 701 |
| Chain | Residue |
| A | ARG317 |
| A | GLN319 |
| A | PHE320 |
| A | ILE331 |
| A | TYR334 |
| A | ARG340 |
| A | GLN417 |
| A | ALA418 |
| A | GLY421 |
| B | PHE146 |
| B | MET148 |
| B | THR149 |
| B | GLY154 |
| B | SER155 |
| B | TRP186 |
| B | ILE187 |
| B | GLY188 |
| B | ASN247 |
| B | VAL439 |
| B | THR442 |
| B | TRP443 |
| B | ASP446 |
| B | ASN448 |
| B | VAL449 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
