1SIR
The Crystal Structure and Mechanism of Human Glutaryl-CoA Dehydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000062 | molecular_function | fatty-acyl-CoA binding |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0004361 | molecular_function | glutaryl-CoA dehydrogenase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006568 | biological_process | L-tryptophan metabolic process |
| A | 0006637 | biological_process | acyl-CoA metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0019395 | biological_process | fatty acid oxidation |
| A | 0033512 | biological_process | L-lysine catabolic process to acetyl-CoA via saccharopine |
| A | 0033514 | biological_process | L-lysine catabolic process to acetyl-CoA via L-pipecolate |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0046949 | biological_process | fatty-acyl-CoA biosynthetic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD A 399 |
| Chain | Residue |
| A | PHE133 |
| A | ARG275 |
| A | PHE278 |
| A | LEU282 |
| A | ASN285 |
| A | GLN286 |
| A | ASP343 |
| A | MET344 |
| A | GLY347 |
| A | ILE350 |
| A | THR372 |
| A | LEU135 |
| A | PHE390 |
| A | NBC400 |
| A | HOH501 |
| A | HOH502 |
| A | HOH506 |
| A | THR136 |
| A | GLY141 |
| A | SER142 |
| A | TRP168 |
| A | ILE169 |
| A | THR170 |
| A | LEU212 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NBC A 400 |
| Chain | Residue |
| A | ARG94 |
| A | SER95 |
| A | LEU103 |
| A | SER142 |
| A | PRO144 |
| A | THR170 |
| A | PHE243 |
| A | GLY244 |
| A | LEU246 |
| A | ASN247 |
| A | ARG250 |
| A | PRO320 |
| A | TYR369 |
| A | GLU370 |
| A | ARG382 |
| A | FAD399 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q60759","evidenceCode":"ECO:0000250"}]} |
| 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 | ALA249 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLU370 |
