1BUC
THREE-DIMENSIONAL STRUCTURE OF BUTYRYL-COA DEHYDROGENASE FROM MEGASPHAERA ELSDENII
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| 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 | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| 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 | 0016937 | molecular_function | short-chain fatty acyl-CoA dehydrogenase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE CAA A 384 |
| Chain | Residue |
| A | THR162 |
| A | ASN182 |
| A | HIS183 |
| A | PHE236 |
| A | MET240 |
| A | MET241 |
| A | LEU243 |
| A | ASP244 |
| A | ARG247 |
| A | THR317 |
| A | TYR366 |
| A | GLU367 |
| A | GLY368 |
| A | FAD385 |
| A | LEU96 |
| A | PHE126 |
| A | THR129 |
| A | GLY134 |
| A | THR135 |
| A | ALA137 |
| A | SER138 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CAA B 384 |
| Chain | Residue |
| B | LEU96 |
| B | THR129 |
| B | GLY134 |
| B | THR135 |
| B | ASN182 |
| B | HIS183 |
| B | PHE236 |
| B | MET240 |
| B | MET241 |
| B | LEU243 |
| B | ASP244 |
| B | ARG247 |
| B | TYR366 |
| B | GLU367 |
| B | GLY368 |
| B | FAD385 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FAD A 385 |
| Chain | Residue |
| A | PHE126 |
| A | LEU128 |
| A | THR129 |
| A | GLY134 |
| A | THR135 |
| A | PHE160 |
| A | THR162 |
| A | ARG272 |
| A | PHE275 |
| A | SER284 |
| A | ILE285 |
| A | GLN340 |
| A | ILE341 |
| A | GLY344 |
| A | ILE362 |
| A | GLU367 |
| A | THR369 |
| A | GLU371 |
| A | MET375 |
| A | CAA384 |
| B | GLN283 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD B 385 |
| Chain | Residue |
| A | GLN283 |
| B | PHE126 |
| B | LEU128 |
| B | THR129 |
| B | GLY134 |
| B | THR135 |
| B | PHE160 |
| B | THR162 |
| B | LYS205 |
| B | ARG272 |
| B | GLN274 |
| B | PHE275 |
| B | LEU279 |
| B | PHE282 |
| B | SER284 |
| B | GLN340 |
| B | ILE341 |
| B | GLY344 |
| B | TYR366 |
| B | GLU367 |
| B | THR369 |
| B | GLU371 |
| B | MET375 |
| B | CAA384 |
| site_id | CA |
| Number of Residues | 1 |
| Details | CATALYTIC BASE, CHAIN A |
| Chain | Residue |
| A | GLU367 |
| site_id | CB |
| Number of Residues | 1 |
| Details | CATALYTIC BASE, CHAIN B |
| Chain | Residue |
| B | GLU367 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"8399220","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLY246 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLY246 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLU367 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLU367 |
