4Y9J
Crystal Structure of Caenorhabditis elegans ACDH-11 in complex with C11-CoA
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 | 37 |
| Details | binding site for residue FAD A 701 |
| Chain | Residue |
| A | GLN206 |
| A | LYS295 |
| A | THR298 |
| A | TRP463 |
| A | GLU464 |
| A | THR466 |
| A | ASN468 |
| A | VAL469 |
| A | LEU472 |
| A | UCC702 |
| A | HOH811 |
| A | MET208 |
| A | HOH813 |
| A | HOH820 |
| A | HOH873 |
| A | HOH877 |
| A | HOH995 |
| A | HOH1035 |
| A | HOH1043 |
| A | HOH1045 |
| B | ARG359 |
| B | VAL361 |
| A | THR209 |
| B | PHE362 |
| B | GLN366 |
| B | HIS372 |
| B | GLU437 |
| B | CYS438 |
| B | GLY440 |
| B | GLY441 |
| B | HOH894 |
| A | GLY213 |
| A | GLY214 |
| A | SER215 |
| A | PHE241 |
| A | SER242 |
| A | SER243 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | binding site for residue UCC A 702 |
| Chain | Residue |
| A | SER161 |
| A | CYS162 |
| A | GLN206 |
| A | MET208 |
| A | THR209 |
| A | GLY214 |
| A | SER215 |
| A | ALA218 |
| A | SER267 |
| A | ARG321 |
| A | VAL323 |
| A | SER327 |
| A | LEU330 |
| A | ASN331 |
| A | ARG334 |
| A | ASN337 |
| A | ALA340 |
| A | TRP463 |
| A | GLU464 |
| A | GLY465 |
| A | ASP473 |
| A | FAD701 |
| A | HOH801 |
| A | HOH803 |
| A | HOH821 |
| A | HOH823 |
| A | HOH885 |
| A | HOH904 |
| A | HOH917 |
| site_id | AC3 |
| Number of Residues | 37 |
| Details | binding site for residue FAD B 701 |
| Chain | Residue |
| B | HOH1011 |
| B | HOH1022 |
| B | HOH1044 |
| B | HOH1109 |
| A | ARG359 |
| A | VAL361 |
| A | PHE362 |
| A | GLN366 |
| A | TRP369 |
| A | HIS372 |
| A | GLU437 |
| A | CYS438 |
| A | GLY440 |
| A | GLY441 |
| A | HOH815 |
| B | GLN206 |
| B | MET208 |
| B | THR209 |
| B | GLY214 |
| B | SER215 |
| B | PHE241 |
| B | SER242 |
| B | SER243 |
| B | LYS295 |
| B | THR298 |
| B | ILE462 |
| B | TRP463 |
| B | THR466 |
| B | ASN468 |
| B | VAL469 |
| B | LEU472 |
| B | UCC702 |
| B | HOH827 |
| B | HOH861 |
| B | HOH927 |
| B | HOH1001 |
| B | HOH1002 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | binding site for residue UCC B 702 |
| Chain | Residue |
| B | SER161 |
| B | ALA165 |
| B | GLN206 |
| B | SER215 |
| B | ALA218 |
| B | SER267 |
| B | ARG321 |
| B | SER327 |
| B | LEU330 |
| B | ASN331 |
| B | ARG334 |
| B | ALA340 |
| B | ARG414 |
| B | TRP463 |
| B | GLU464 |
| B | GLY465 |
| B | VAL469 |
| B | ARG476 |
| B | FAD701 |
| B | HOH825 |
| B | HOH829 |
| B | HOH844 |
| B | HOH872 |
| B | HOH889 |
| B | HOH896 |
| B | HOH946 |
| B | HOH966 |
| B | HOH996 |
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 |
