4Y9L
Crystal Structure of Caenorhabditis elegans ACDH-11
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 1990845 | biological_process | adaptive thermogenesis |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0005504 | molecular_function | fatty acid binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 1990845 | biological_process | adaptive thermogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue FAD A 701 |
| Chain | Residue |
| A | GLN206 |
| A | ILE462 |
| A | TRP463 |
| A | GLU464 |
| A | THR466 |
| A | ASN468 |
| A | VAL469 |
| A | LEU472 |
| A | HOH807 |
| A | HOH834 |
| A | HOH836 |
| A | MET208 |
| A | HOH866 |
| A | HOH867 |
| A | HOH943 |
| B | ARG359 |
| B | VAL361 |
| B | PHE362 |
| B | GLN366 |
| B | GLU437 |
| B | CYS438 |
| B | GLY440 |
| A | THR209 |
| B | GLY441 |
| B | HOH845 |
| A | GLY214 |
| A | SER215 |
| A | PHE241 |
| A | SER242 |
| A | SER243 |
| A | LYS295 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | binding site for residue FAD B 701 |
| Chain | Residue |
| A | ARG359 |
| A | VAL361 |
| A | PHE362 |
| A | GLN366 |
| A | TRP369 |
| A | GLU437 |
| A | CYS438 |
| A | GLY440 |
| A | GLY441 |
| A | HOH811 |
| B | GLN206 |
| B | MET208 |
| B | THR209 |
| B | GLY214 |
| B | SER215 |
| B | PHE241 |
| B | SER242 |
| B | SER243 |
| B | TRP463 |
| B | GLU464 |
| B | THR466 |
| B | ASN468 |
| B | VAL469 |
| B | LEU472 |
| B | HOH814 |
| B | HOH832 |
| B | HOH843 |
| B | HOH850 |
| B | HOH907 |
| B | HOH951 |
| B | HOH956 |
| B | HOH964 |
| B | HOH968 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PDB","id":"4Y9J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y9L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4Y9J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4Y9J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y9L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"4Y9L","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
