1K39
The structure of yeast delta3-delta2-enoyl-COA isomerase complexed with octanoyl-COA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005782 | cellular_component | peroxisomal matrix |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0016853 | molecular_function | isomerase activity |
| B | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005782 | cellular_component | peroxisomal matrix |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0016853 | molecular_function | isomerase activity |
| C | 0004165 | molecular_function | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005782 | cellular_component | peroxisomal matrix |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006635 | biological_process | fatty acid beta-oxidation |
| C | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 281 |
| Chain | Residue |
| A | TYR225 |
| A | PRO227 |
| B | TYR258 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 C 281 |
| Chain | Residue |
| B | TYR225 |
| C | LYS257 |
| C | TYR258 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 282 |
| Chain | Residue |
| C | PRO227 |
| A | LYS257 |
| A | TYR258 |
| C | TYR225 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CO8 A 300 |
| Chain | Residue |
| A | ASP28 |
| A | ASN29 |
| A | LEU30 |
| A | ALA32 |
| A | GLY35 |
| A | SER68 |
| A | ALA70 |
| A | ASP71 |
| A | PHE72 |
| A | PHE97 |
| A | ARG100 |
| A | ASN101 |
| A | ILE124 |
| A | GLY125 |
| A | LEU126 |
| A | LEU153 |
| A | GLU158 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CO8 B 301 |
| Chain | Residue |
| B | LEU30 |
| B | ALA32 |
| B | SER68 |
| B | ALA70 |
| B | ASP71 |
| B | LYS73 |
| B | PHE97 |
| B | ARG100 |
| B | ASN101 |
| B | ILE124 |
| B | GLY125 |
| B | LEU126 |
| B | LEU153 |
| B | LEU155 |
| B | GLU158 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CO8 C 302 |
| Chain | Residue |
| C | ASP28 |
| C | ASN29 |
| C | LEU30 |
| C | ALA32 |
| C | SER68 |
| C | ALA70 |
| C | ASP71 |
| C | PHE72 |
| C | LYS73 |
| C | PHE97 |
| C | ARG100 |
| C | ASN101 |
| C | ILE124 |
| C | GLY125 |
| C | LEU126 |
| C | LEU155 |
| C | GLU158 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"26527136","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26527136","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZDB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZDC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26527136","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZDC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pjh |
| Chain | Residue | Details |
| A | LEU126 | |
| A | GLU158 | |
| A | ALA70 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pjh |
| Chain | Residue | Details |
| B | LEU126 | |
| B | GLU158 | |
| B | ALA70 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1pjh |
| Chain | Residue | Details |
| C | LEU126 | |
| C | GLU158 | |
| C | ALA70 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 499 |
| Chain | Residue | Details |
| A | ALA70 | electrostatic stabiliser |
| A | ASN101 | electrostatic stabiliser, modifies pKa |
| A | LEU126 | electrostatic stabiliser |
| A | GLU158 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 499 |
| Chain | Residue | Details |
| B | ALA70 | electrostatic stabiliser |
| B | ASN101 | electrostatic stabiliser, modifies pKa |
| B | LEU126 | electrostatic stabiliser |
| B | GLU158 | proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 499 |
| Chain | Residue | Details |
| C | ALA70 | electrostatic stabiliser |
| C | ASN101 | electrostatic stabiliser, modifies pKa |
| C | LEU126 | electrostatic stabiliser |
| C | GLU158 | proton acceptor, proton donor |
