5CT6
Wild-type Bacillus subtilis lipase A with 20% [BMIM][Cl]
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 | 5 |
| Details | binding site for residue CL A 201 |
| Chain | Residue |
| A | GLY155 |
| A | HIS156 |
| A | ILE157 |
| A | GLY158 |
| B | GLY155 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue BM0 A 202 |
| Chain | Residue |
| A | SER77 |
| A | HIS156 |
| A | HOH305 |
| A | ILE12 |
| A | GLY13 |
| A | GLY14 |
| A | ASN18 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue BM0 A 203 |
| Chain | Residue |
| A | TYR49 |
| A | ASN50 |
| A | HOH302 |
| B | HIS3 |
| B | LYS35 |
| B | THR66 |
| B | GLY67 |
| B | ALA68 |
| B | MET137 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue BM0 A 204 |
| Chain | Residue |
| A | THR45 |
| A | THR47 |
| A | HOH396 |
| B | LEU108 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue BM0 A 205 |
| Chain | Residue |
| A | GLY116 |
| A | ASP118 |
| A | PRO119 |
| A | LYS122 |
| A | HOH375 |
| B | HOH348 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue BM0 A 206 |
| Chain | Residue |
| A | ASP34 |
| A | LEU36 |
| A | TYR37 |
| A | ARG107 |
| A | ARG142 |
| A | ASP144 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 201 |
| Chain | Residue |
| A | GLY155 |
| A | HOH306 |
| B | HIS156 |
| B | ILE157 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 202 |
| Chain | Residue |
| B | THR47 |
| B | ASN48 |
| B | HOH380 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue BM0 B 203 |
| Chain | Residue |
| A | ILE157 |
| B | TRP42 |
| B | GLY158 |
| B | TYR161 |
| B | HOH367 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue BM0 B 204 |
| Chain | Residue |
| B | ASP34 |
| B | LEU36 |
| B | TYR37 |
| B | ARG107 |
| B | ARG142 |
| B | ASP144 |
| B | HOH381 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue BM0 B 205 |
| Chain | Residue |
| A | TYR161 |
| B | PHE17 |
| B | TYR161 |
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 |
