Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| B | 0003824 | molecular_function | catalytic activity |
| C | 0003824 | molecular_function | catalytic activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CO8 B 701 |
| Chain | Residue |
| B | PRO24 |
| B | GLY111 |
| B | ASN135 |
| B | ILE142 |
| B | TYR251 |
| B | LEU255 |
| B | LYS256 |
| B | LYS259 |
| B | VAL25 |
| B | VAL61 |
| B | ALA64 |
| B | LEU66 |
| B | ASP67 |
| B | LEU68 |
| B | PRO109 |
| B | ALA110 |
Functional Information from PROSITE/UniProt
| site_id | PS00166 |
| Number of Residues | 21 |
| Details | ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. VSaINGacpAGGclvaLtCDY |
| Chain | Residue | Details |
| A | VAL101-TYR121 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15351645","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SG4","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"15351645","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P42125","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P42125","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| A | GLU136 | |
| A | PRO144 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| B | GLU136 | |
| B | PRO144 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dci |
| Chain | Residue | Details |
| C | GLU136 | |
| C | PRO144 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 341 |
| Chain | Residue | Details |
| A | LEU66 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY111 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN135 | electrostatic stabiliser, modifies pKa |
| A | GLU136 | polar/non-polar interaction, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 341 |
| Chain | Residue | Details |
| B | LEU66 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY111 | electrostatic stabiliser, hydrogen bond donor |
| B | ASN135 | electrostatic stabiliser, modifies pKa |
| B | GLU136 | polar/non-polar interaction, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 341 |
| Chain | Residue | Details |
| C | LEU66 | electrostatic stabiliser, hydrogen bond donor |
| C | GLY111 | electrostatic stabiliser, hydrogen bond donor |
| C | ASN135 | electrostatic stabiliser, modifies pKa |
| C | GLU136 | polar/non-polar interaction, proton acceptor, proton donor |
