1R4Z
Bacillus subtilis lipase A with covalently bound Rc-IPG-phosphonate-inhibitor
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 | 7 |
| Details | BINDING SITE FOR RESIDUE RIL A 277 |
| Chain | Residue |
| A | GLY11 |
| A | ILE12 |
| A | GLY14 |
| A | HIS76 |
| A | SER77 |
| A | MET78 |
| A | HIS156 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE RIL B 277 |
| Chain | Residue |
| B | HIS76 |
| B | SER77 |
| B | MET78 |
| B | HIS156 |
| B | GLY11 |
| B | ILE12 |
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 | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 11491291, 12077437 |
| Chain | Residue | Details |
| A | ASP133 | |
| A | HIS156 | |
| A | MET78 | |
| A | SER77 | |
| A | ILE12 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 11491291, 12077437 |
| Chain | Residue | Details |
| B | ASP133 | |
| B | HIS156 | |
| B | MET78 | |
| B | SER77 | |
| B | 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 | 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 |
