1PJH
Structural studies on delta3-delta2-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily
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 | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 500 |
| Chain | Residue |
| C | GLY63 |
| C | ASN205 |
| C | ALA206 |
| C | GLU207 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | HOH1422 |
| A | HOH1435 |
| B | HOH1435 |
| A | GLY63 |
| A | ASN205 |
| A | ALA206 |
| A | GLU207 |
| A | HOH1419 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| B | ASN141 |
| B | ASN200 |
| B | MET201 |
| B | PRO202 |
| B | SO4503 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 503 |
| Chain | Residue |
| B | ARG64 |
| B | LYS143 |
| B | PRO202 |
| B | SER203 |
| B | SER204 |
| B | SO4502 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 504 |
| Chain | Residue |
| C | ARG64 |
| C | LYS143 |
| C | SER203 |
| C | SER204 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 505 |
| Chain | Residue |
| C | ARG64 |
| C | LYS143 |
| C | SER203 |
| C | HOH1342 |
| C | HOH1398 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 506 |
| Chain | Residue |
| A | ARG64 |
| A | LYS143 |
| A | SER203 |
| A | SER204 |
| A | SO4508 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 507 |
| Chain | Residue |
| B | TYR225 |
| B | PRO227 |
| B | HOH1427 |
| C | LYS257 |
| C | TYR258 |
| C | ASP261 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 508 |
| Chain | Residue |
| A | ASN141 |
| A | ASN200 |
| A | MET201 |
| A | PRO202 |
| A | SO4506 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 509 |
| Chain | Residue |
| A | TYR225 |
| A | PRO227 |
| B | LYS257 |
| B | TYR258 |
| B | ASP261 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1301 |
| Chain | Residue |
| A | GLY69 |
| A | ALA70 |
| A | GLY125 |
| A | LEU126 |
| A | LEU155 |
| A | GLU158 |
| A | HOH1432 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1302 |
| Chain | Residue |
| B | GLY69 |
| B | ALA70 |
| B | GLY125 |
| B | LEU126 |
| B | LEU155 |
| B | GLU158 |
| B | HOH1394 |
| B | HOH1415 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 1303 |
| Chain | Residue |
| C | ALA70 |
| C | ARG100 |
| C | GLY125 |
| C | LEU126 |
| C | GLU158 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1304 |
| Chain | Residue |
| A | ILE195 |
| A | SER196 |
| A | HOH1364 |
| B | GLU176 |
| B | LYS182 |
| B | ILE188 |
| B | HOH1418 |
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 |
