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 | 5 |
Details | binding site for residue SO4 A 301 |
Chain | Residue |
A | ARG64 |
A | LYS143 |
A | PRO202 |
A | SER203 |
A | SER204 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | HOH406 |
A | HOH461 |
A | SER62 |
A | GLY63 |
A | ALA206 |
A | GLU207 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | TYR225 |
A | PRO227 |
B | LYS257 |
B | ASP261 |
site_id | AC4 |
Number of Residues | 20 |
Details | binding site for residue CO8 A 304 |
Chain | Residue |
A | ASP28 |
A | ASN29 |
A | LEU30 |
A | ALA32 |
A | PHE65 |
A | SER68 |
A | GLY69 |
A | ALA70 |
A | ASP71 |
A | PHE72 |
A | LYS73 |
A | PHE97 |
A | ARG100 |
A | ASN101 |
A | ILE124 |
A | GLY125 |
A | LEU126 |
A | LEU153 |
A | GLU158 |
A | GOL305 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | ALA70 |
A | GLY125 |
A | LEU126 |
A | PHE150 |
A | LEU155 |
A | GLU158 |
A | CO8304 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL A 306 |
Chain | Residue |
A | ILE109 |
A | LEU133 |
A | LYS168 |
A | PHE244 |
A | HOH409 |
A | HOH459 |
A | HOH467 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
B | SER62 |
B | GLY63 |
B | ASN205 |
B | ALA206 |
B | GLU207 |
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 | 5 |
Details | binding site for residue SO4 B 303 |
Chain | Residue |
B | ARG64 |
B | LYS143 |
B | SER203 |
B | HOH422 |
B | HOH427 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residue CO8 B 304 |
Chain | Residue |
B | ASN29 |
B | LEU30 |
B | ALA32 |
B | PHE65 |
B | SER68 |
B | ALA70 |
B | ASP71 |
B | PHE72 |
B | LYS73 |
B | ILE124 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 305 |
Chain | Residue |
B | ALA70 |
B | ARG100 |
B | GLY125 |
B | LEU126 |
B | PHE150 |
B | GLU158 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue GOL B 306 |
Chain | Residue |
B | ILE109 |
B | LEU133 |
B | LYS237 |
B | PHE244 |
B | HOH402 |
B | HOH426 |
B | HOH439 |
C | HOH409 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue GOL B 307 |
Chain | Residue |
B | HIS240 |
C | HIS240 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 301 |
Chain | Residue |
C | ARG64 |
C | LYS143 |
C | PRO202 |
C | SER203 |
C | SER204 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 302 |
Chain | Residue |
A | LYS257 |
A | TYR258 |
C | TYR225 |
site_id | AD7 |
Number of Residues | 7 |
Details | binding site for residue SO4 C 303 |
Chain | Residue |
C | GLY63 |
C | ASN205 |
C | ALA206 |
C | GLU207 |
C | HOH484 |
C | HOH491 |
C | SER62 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 304 |
Chain | Residue |
B | TYR225 |
C | LYS257 |
C | TYR258 |
site_id | AD9 |
Number of Residues | 16 |
Details | binding site for residue CO8 C 305 |
Chain | Residue |
C | ASP28 |
C | ASN29 |
C | LEU30 |
C | SER68 |
C | ALA70 |
C | ASP71 |
C | PHE72 |
C | LYS73 |
C | ASN96 |
C | PHE97 |
C | ARG100 |
C | ASN101 |
C | GLY125 |
C | LEU126 |
C | GLU158 |
C | GOL307 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue GOL C 306 |
Chain | Residue |
C | GLU16 |
C | LEU214 |
site_id | AE2 |
Number of Residues | 7 |
Details | binding site for residue GOL C 307 |
Chain | Residue |
C | ALA70 |
C | GLY125 |
C | LEU126 |
C | PHE150 |
C | LEU155 |
C | GLU158 |
C | CO8305 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue GOL C 308 |
Chain | Residue |
A | HOH419 |
C | ILE109 |
C | LEU133 |
C | LYS237 |
C | HOH402 |
C | HOH454 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU158 | |
B | GLU158 | |
C | GLU158 | |
Chain | Residue | Details |
A | SER68 | |
B | SER68 | |
C | SER68 | |
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 |