9RGQ
Crystal Structure of Rattus norvegicus Enoyl-CoA Hydratase in unliganded form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| A | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006574 | biological_process | L-valine catabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0018812 | molecular_function | 3-hydroxyacyl-CoA dehydratase activity |
| A | 0019477 | biological_process | L-lysine catabolic process |
| A | 0043956 | molecular_function | 3-hydroxypropionyl-CoA dehydratase activity |
| A | 0120092 | molecular_function | (2E)-butenoyl-CoA hydratase activity |
| B | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| B | 0004300 | molecular_function | enoyl-CoA hydratase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006574 | biological_process | L-valine catabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0018812 | molecular_function | 3-hydroxyacyl-CoA dehydratase activity |
| B | 0019477 | biological_process | L-lysine catabolic process |
| B | 0043956 | molecular_function | 3-hydroxypropionyl-CoA dehydratase activity |
| B | 0120092 | molecular_function | (2E)-butenoyl-CoA hydratase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAaVNGyalGGGcelaMmCDI |
| Chain | Residue | Details |
| A | ILE131-ILE151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8BH95","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BH95","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BH95","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 315 |
| Chain | Residue | Details |
| A | ALA98 | activator, electrostatic stabiliser |
| A | GLY141 | activator, electrostatic stabiliser |
| A | GLU144 | hydrogen bond acceptor, increase basicity |
| A | GLU164 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 315 |
| Chain | Residue | Details |
| B | ALA98 | activator, electrostatic stabiliser |
| B | GLY141 | activator, electrostatic stabiliser |
| B | GLU144 | hydrogen bond acceptor, increase basicity |
| B | GLU164 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
