3QZU
Crystal structure of Bacillus subtilis Lipase A 7-fold mutant; the outcome of directed evolution towards thermostability
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004806 | molecular_function | triacylglycerol 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 |
| B | 0004806 | molecular_function | triacylglycerol lipase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016298 | molecular_function | lipase activity |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 182 |
| Chain | Residue |
| A | ILE12 |
| A | SER77 |
| A | MET78 |
| A | HOH272 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 183 |
| Chain | Residue |
| A | TRP42 |
| A | VAL54 |
| A | ARG57 |
| A | HOH246 |
| A | HOH360 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 184 |
| Chain | Residue |
| A | MET137 |
| A | ASN138 |
| A | CYS139 |
| A | ARG142 |
| B | ARG107 |
| B | HOH264 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 185 |
| Chain | Residue |
| A | ARG107 |
| A | ASP144 |
| B | ARG142 |
| B | HOH309 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 186 |
| Chain | Residue |
| A | SER162 |
| A | SER163 |
| A | GLN164 |
| A | HOH201 |
| A | HOH477 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 182 |
| Chain | Residue |
| B | ILE12 |
| B | SER77 |
| B | MET78 |
| B | HOH314 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 183 |
| Chain | Residue |
| B | TRP42 |
| B | ARG57 |
| B | HOH240 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 184 |
| Chain | Residue |
| B | SER162 |
| B | SER163 |
| B | GLN164 |
| B | HOH371 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 185 |
| Chain | Residue |
| B | ILE135 |
| B | HOH209 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"11491291","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11583117","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12077437","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11491291","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11583117","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12077437","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
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 |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| B | ILE12 | electrostatic stabiliser |
| B | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | MET78 | electrostatic stabiliser |
| B | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| B | HIS156 | proton acceptor, proton donor |
