4H0C
Crystal structure of phospholipase/Carboxylesterase from Dyadobacter fermentans DSM 18053
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0008474 | molecular_function | palmitoyl-(protein) hydrolase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0052689 | molecular_function | carboxylic ester hydrolase activity |
A | 0098734 | biological_process | macromolecule depalmitoylation |
B | 0005737 | cellular_component | cytoplasm |
B | 0008474 | molecular_function | palmitoyl-(protein) hydrolase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0052689 | molecular_function | carboxylic ester hydrolase activity |
B | 0098734 | biological_process | macromolecule depalmitoylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIT A 301 |
Chain | Residue |
A | ARG28 |
A | HIS161 |
A | VAL162 |
A | HIS191 |
A | HOH403 |
B | GOL303 |
B | HOH471 |
A | TYR60 |
A | SER63 |
A | PHE64 |
A | SER105 |
A | GLN106 |
A | CYS109 |
A | THR129 |
A | GLY130 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 302 |
Chain | Residue |
A | TYR100 |
A | ILE205 |
A | LEU206 |
A | LYS207 |
A | HOH466 |
A | HOH510 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CIT B 301 |
Chain | Residue |
A | PRO160 |
B | ARG28 |
B | TYR60 |
B | SER63 |
B | PHE64 |
B | SER105 |
B | GLN106 |
B | CYS109 |
B | THR129 |
B | GLY130 |
B | HIS161 |
B | VAL162 |
B | HIS191 |
B | HOH462 |
B | HOH499 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 302 |
Chain | Residue |
B | GLN39 |
B | LEU42 |
B | HOH411 |
B | HOH451 |
B | HOH469 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 303 |
Chain | Residue |
A | ARG28 |
A | SER63 |
A | HIS161 |
A | CIT301 |
B | SER63 |
B | HOH419 |
B | HOH471 |