5CRI
Wild-type Bacillus subtilis lipase A with 0% [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 | 4 |
| Details | binding site for residue SO4 A 201 |
| Chain | Residue |
| A | VAL154 |
| A | SER162 |
| A | SER163 |
| A | GLN164 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | HOH446 |
| B | ARG33 |
| B | MET137 |
| B | TYR139 |
| A | ARG142 |
| A | HOH304 |
| A | HOH355 |
| A | HOH398 |
| A | HOH441 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | LYS122 |
| A | GLY155 |
| A | HIS156 |
| A | ILE157 |
| A | GLY158 |
| A | ASN181 |
| A | HOH330 |
| A | HOH351 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 204 |
| Chain | Residue |
| A | ASN50 |
| A | HOH314 |
| A | HOH323 |
| A | HOH449 |
| B | SER162 |
| B | SER163 |
| B | HOH331 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 201 |
| Chain | Residue |
| B | TYR129 |
| B | ARG142 |
| B | GLN150 |
| B | HOH305 |
| B | HOH327 |
| B | HOH383 |
| B | HOH393 |
| B | HOH411 |
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 |
