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3QMM

Structure of 6B, a thermostable mutant of Bacillus subtilis lipase obtained through directed evolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriglyceride lipase activity
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
B0004806molecular_functiontriglyceride lipase activity
B0005576cellular_componentextracellular region
B0006629biological_processlipid metabolic process
B0016042biological_processlipid catabolic process
B0016298molecular_functionlipase activity
B0016787molecular_functionhydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437
ChainResidueDetails
ASER77
BSER77

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:11491291, ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437
ChainResidueDetails
AASP133
AHIS156
BASP133
BHIS156

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 518
ChainResidueDetails
AILE12electrostatic stabiliser
ASER77covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
AMET78electrostatic stabiliser
AASP133electrostatic stabiliser, increase basicity, modifies pKa
AHIS156proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 518
ChainResidueDetails
BILE12electrostatic stabiliser
BSER77covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
BMET78electrostatic stabiliser
BASP133electrostatic stabiliser, increase basicity, modifies pKa
BHIS156proton acceptor, proton donor

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PDB entries from 2024-04-24

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