3D2A
Structure of 1-17A4, a thermostable mutant of Bacillus subtilis lipase obtained through directed evolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004806 | molecular_function | triglyceride lipase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006629 | biological_process | lipid metabolic process |
A | 0016042 | biological_process | lipid catabolic process |
A | 0016298 | molecular_function | lipase activity |
A | 0016787 | molecular_function | hydrolase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437 |
Chain | Residue | Details |
A | SER77 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437 |
Chain | Residue | Details |
A | ASP133 | |
A | HIS156 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 518 |
Chain | Residue | Details |
A | ILE12 | electrostatic stabiliser |
A | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
A | MET78 | electrostatic stabiliser |
A | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
A | HIS156 | proton acceptor, proton donor |