1JQI
Crystal Structure of Rat Short Chain Acyl-CoA Dehydrogenase Complexed With Acetoacetyl-CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| 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 | 0031966 | cellular_component | mitochondrial membrane |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0042594 | biological_process | response to starvation |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046359 | biological_process | butyrate catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0051384 | biological_process | response to glucocorticoid |
| A | 0071949 | molecular_function | FAD binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| 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 | 0031966 | cellular_component | mitochondrial membrane |
| B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| B | 0042594 | biological_process | response to starvation |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046359 | biological_process | butyrate catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0051384 | biological_process | response to glucocorticoid |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE CAA A 400 |
| Chain | Residue |
| A | VAL94 |
| A | LEU244 |
| A | ASP245 |
| A | ARG248 |
| A | THR318 |
| A | TYR367 |
| A | GLU368 |
| A | GLY369 |
| A | FAD399 |
| A | HOH1018 |
| A | HOH1023 |
| A | LEU98 |
| A | HOH1219 |
| A | HOH1257 |
| A | GLY136 |
| A | SER137 |
| A | ALA139 |
| A | ASN183 |
| A | PHE237 |
| A | MET241 |
| A | GLN242 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAA B 800 |
| Chain | Residue |
| B | VAL494 |
| B | LEU498 |
| B | GLY536 |
| B | SER537 |
| B | ALA539 |
| B | ASN583 |
| B | PHE637 |
| B | MET641 |
| B | GLN642 |
| B | LEU644 |
| B | ASP645 |
| B | ARG648 |
| B | THR718 |
| B | TYR767 |
| B | GLU768 |
| B | GLY769 |
| B | FAD799 |
| B | HOH1067 |
| B | HOH1089 |
| B | HOH1133 |
| B | HOH1135 |
| B | HOH1178 |
| B | HOH1204 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 399 |
| Chain | Residue |
| A | PHE128 |
| A | LEU130 |
| A | SER131 |
| A | GLY136 |
| A | SER137 |
| A | TRP161 |
| A | THR163 |
| A | GLN284 |
| A | ILE363 |
| A | THR370 |
| A | GLU372 |
| A | LEU376 |
| A | CAA400 |
| A | HOH1024 |
| A | HOH1026 |
| A | HOH1032 |
| A | HOH1074 |
| A | HOH1103 |
| B | ARG673 |
| B | PHE676 |
| B | LEU680 |
| B | LEU683 |
| B | GLN741 |
| B | ILE742 |
| B | GLY745 |
| B | HOH1004 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD B 799 |
| Chain | Residue |
| A | ARG273 |
| A | PHE276 |
| A | LEU283 |
| A | GLN341 |
| A | ILE342 |
| A | GLY345 |
| A | HOH1027 |
| B | PHE528 |
| B | LEU530 |
| B | SER531 |
| B | GLY536 |
| B | SER537 |
| B | TRP561 |
| B | THR563 |
| B | GLN684 |
| B | ILE763 |
| B | THR770 |
| B | GLU772 |
| B | LEU776 |
| B | CAA800 |
| B | HOH1002 |
| B | HOH1011 |
| B | HOH1054 |
| B | HOH1060 |
| B | HOH1072 |
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":"11812788","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11812788","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q07417","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q07417","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 | GLY247 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLY647 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLU368 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLU768 |
