4ZDE
Crystal structure of yeast D3,D2-enoyl-CoA isomerase F268A mutant
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 | 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 | 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 | 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 | 8 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | ALA70 |
| A | PHE97 |
| A | ARG100 |
| A | GLY125 |
| A | LEU126 |
| A | LEU155 |
| A | GLU158 |
| A | HOH403 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | PRO202 |
| A | SER203 |
| A | SER204 |
| A | ARG64 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | SER62 |
| A | GLY63 |
| A | ALA206 |
| A | GLU207 |
| A | HOH419 |
| A | HOH467 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 304 |
| Chain | Residue |
| A | TYR225 |
| A | PRO227 |
| A | HOH452 |
| B | LYS257 |
| B | ASP261 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 305 |
| Chain | Residue |
| A | LYS257 |
| A | TYR258 |
| C | TYR225 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 306 |
| Chain | Residue |
| A | GLU9 |
| A | ILE25 |
| A | ASN26 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 301 |
| Chain | Residue |
| B | ALA70 |
| B | PHE97 |
| B | ARG100 |
| B | GLY125 |
| B | LEU126 |
| B | PHE150 |
| B | LEU155 |
| B | GLU158 |
| B | HOH456 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| B | ARG64 |
| B | LYS143 |
| B | PRO202 |
| B | SER203 |
| B | SER204 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| B | SER62 |
| B | GLY63 |
| B | ALA206 |
| B | GLU207 |
| B | SO4304 |
| B | HOH405 |
| B | HOH411 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 304 |
| Chain | Residue |
| B | SO4303 |
| B | HOH422 |
| B | HOH446 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 305 |
| Chain | Residue |
| B | GLU9 |
| B | ILE25 |
| B | ASN26 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL C 301 |
| Chain | Residue |
| C | GLY69 |
| C | ALA70 |
| C | ARG100 |
| C | GLY125 |
| C | LEU126 |
| C | LEU155 |
| C | GLU158 |
| C | HOH425 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 302 |
| Chain | Residue |
| C | ARG64 |
| C | LYS143 |
| C | PRO202 |
| C | SER203 |
| C | SER204 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 303 |
| Chain | Residue |
| C | GLY63 |
| C | SER204 |
| C | ALA206 |
| C | GLU207 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 304 |
| Chain | Residue |
| C | SER12 |
| C | HIS23 |
| C | ILE25 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 305 |
| Chain | Residue |
| B | TYR225 |
| B | PRO227 |
| C | LYS257 |
| C | TYR258 |
| C | ASP261 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 306 |
| Chain | Residue |
| C | GLU9 |
| C | ASN26 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:26527136 |
| Chain | Residue | Details |
| A | GLU158 | |
| B | GLU158 | |
| C | GLU158 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26527136, ECO:0007744|PDB:4ZDB, ECO:0007744|PDB:4ZDC |
| Chain | Residue | Details |
| A | SER68 | |
| B | SER68 | |
| C | SER68 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26527136, ECO:0007744|PDB:4ZDC |
| Chain | Residue | Details |
| A | LEU126 | |
| B | LEU126 | |
| C | LEU126 |
Catalytic Information from CSA
| 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 |
