3D2C
Structure of 4D3, a thermostable mutant of Bacillus subtilis lipase obtained through directed evolution
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 |
| C | 0004806 | molecular_function | triacylglycerol lipase activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0016042 | biological_process | lipid catabolic process |
| C | 0016298 | molecular_function | lipase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0004806 | molecular_function | triacylglycerol lipase activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0016042 | biological_process | lipid catabolic process |
| D | 0016298 | molecular_function | lipase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| E | 0004806 | molecular_function | triacylglycerol lipase activity |
| E | 0005576 | cellular_component | extracellular region |
| E | 0006629 | biological_process | lipid metabolic process |
| E | 0016042 | biological_process | lipid catabolic process |
| E | 0016298 | molecular_function | lipase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| F | 0004806 | molecular_function | triacylglycerol lipase activity |
| F | 0005576 | cellular_component | extracellular region |
| F | 0006629 | biological_process | lipid metabolic process |
| F | 0016042 | biological_process | lipid catabolic process |
| F | 0016298 | molecular_function | lipase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| G | 0004806 | molecular_function | triacylglycerol lipase activity |
| G | 0005576 | cellular_component | extracellular region |
| G | 0006629 | biological_process | lipid metabolic process |
| G | 0016042 | biological_process | lipid catabolic process |
| G | 0016298 | molecular_function | lipase activity |
| G | 0016787 | molecular_function | hydrolase activity |
| H | 0004806 | molecular_function | triacylglycerol lipase activity |
| H | 0005576 | cellular_component | extracellular region |
| H | 0006629 | biological_process | lipid metabolic process |
| H | 0016042 | biological_process | lipid catabolic process |
| H | 0016298 | molecular_function | lipase activity |
| H | 0016787 | molecular_function | hydrolase activity |
| I | 0004806 | molecular_function | triacylglycerol lipase activity |
| I | 0005576 | cellular_component | extracellular region |
| I | 0006629 | biological_process | lipid metabolic process |
| I | 0016042 | biological_process | lipid catabolic process |
| I | 0016298 | molecular_function | lipase activity |
| I | 0016787 | molecular_function | hydrolase activity |
| J | 0004806 | molecular_function | triacylglycerol lipase activity |
| J | 0005576 | cellular_component | extracellular region |
| J | 0006629 | biological_process | lipid metabolic process |
| J | 0016042 | biological_process | lipid catabolic process |
| J | 0016298 | molecular_function | lipase activity |
| J | 0016787 | molecular_function | hydrolase activity |
| K | 0004806 | molecular_function | triacylglycerol lipase activity |
| K | 0005576 | cellular_component | extracellular region |
| K | 0006629 | biological_process | lipid metabolic process |
| K | 0016042 | biological_process | lipid catabolic process |
| K | 0016298 | molecular_function | lipase activity |
| K | 0016787 | molecular_function | hydrolase activity |
| L | 0004806 | molecular_function | triacylglycerol lipase activity |
| L | 0005576 | cellular_component | extracellular region |
| L | 0006629 | biological_process | lipid metabolic process |
| L | 0016042 | biological_process | lipid catabolic process |
| L | 0016298 | molecular_function | lipase activity |
| L | 0016787 | molecular_function | hydrolase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| 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 | 24 |
| 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 | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| A | ASP133 | |
| A | HIS156 | |
| A | MET78 | |
| A | SER77 | |
| A | ILE12 |
| site_id | CSA10 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| J | ASP133 | |
| J | HIS156 | |
| J | MET78 | |
| J | SER77 | |
| J | ILE12 |
| site_id | CSA11 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| K | ASP133 | |
| K | HIS156 | |
| K | MET78 | |
| K | SER77 | |
| K | ILE12 |
| site_id | CSA12 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| L | ASP133 | |
| L | HIS156 | |
| L | MET78 | |
| L | SER77 | |
| L | ILE12 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| B | ASP133 | |
| B | HIS156 | |
| B | MET78 | |
| B | SER77 | |
| B | ILE12 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| C | ASP133 | |
| C | HIS156 | |
| C | MET78 | |
| C | SER77 | |
| C | ILE12 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| D | ASP133 | |
| D | HIS156 | |
| D | MET78 | |
| D | SER77 | |
| D | ILE12 |
| site_id | CSA5 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| E | ASP133 | |
| E | HIS156 | |
| E | MET78 | |
| E | SER77 | |
| E | ILE12 |
| site_id | CSA6 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| F | ASP133 | |
| F | HIS156 | |
| F | MET78 | |
| F | SER77 | |
| F | ILE12 |
| site_id | CSA7 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| G | ASP133 | |
| G | HIS156 | |
| G | MET78 | |
| G | SER77 | |
| G | ILE12 |
| site_id | CSA8 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| H | ASP133 | |
| H | HIS156 | |
| H | MET78 | |
| H | SER77 | |
| H | ILE12 |
| site_id | CSA9 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1r4z |
| Chain | Residue | Details |
| I | ASP133 | |
| I | HIS156 | |
| I | MET78 | |
| I | SER77 | |
| I | ILE12 |
| 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 | MCSA10 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| J | ILE12 | electrostatic stabiliser |
| J | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| J | MET78 | electrostatic stabiliser |
| J | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| J | HIS156 | proton acceptor, proton donor |
| site_id | MCSA11 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| K | ILE12 | electrostatic stabiliser |
| K | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| K | MET78 | electrostatic stabiliser |
| K | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| K | HIS156 | proton acceptor, proton donor |
| site_id | MCSA12 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| L | ILE12 | electrostatic stabiliser |
| L | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| L | MET78 | electrostatic stabiliser |
| L | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| L | 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 |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| C | ILE12 | electrostatic stabiliser |
| C | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | MET78 | electrostatic stabiliser |
| C | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| C | HIS156 | proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| D | ILE12 | electrostatic stabiliser |
| D | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | MET78 | electrostatic stabiliser |
| D | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| D | HIS156 | proton acceptor, proton donor |
| site_id | MCSA5 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| E | ILE12 | electrostatic stabiliser |
| E | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| E | MET78 | electrostatic stabiliser |
| E | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| E | HIS156 | proton acceptor, proton donor |
| site_id | MCSA6 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| F | ILE12 | electrostatic stabiliser |
| F | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| F | MET78 | electrostatic stabiliser |
| F | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| F | HIS156 | proton acceptor, proton donor |
| site_id | MCSA7 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| G | ILE12 | electrostatic stabiliser |
| G | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| G | MET78 | electrostatic stabiliser |
| G | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| G | HIS156 | proton acceptor, proton donor |
| site_id | MCSA8 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| H | ILE12 | electrostatic stabiliser |
| H | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| H | MET78 | electrostatic stabiliser |
| H | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| H | HIS156 | proton acceptor, proton donor |
| site_id | MCSA9 |
| Number of Residues | 5 |
| Details | M-CSA 518 |
| Chain | Residue | Details |
| I | ILE12 | electrostatic stabiliser |
| I | SER77 | covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor |
| I | MET78 | electrostatic stabiliser |
| I | ASP133 | electrostatic stabiliser, increase basicity, modifies pKa |
| I | HIS156 | proton acceptor, proton donor |
