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3QZU

Crystal structure of Bacillus subtilis Lipase A 7-fold mutant; the outcome of directed evolution towards thermostability

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 PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 182
ChainResidue
AILE12
ASER77
AMET78
AHOH272

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 183
ChainResidue
ATRP42
AVAL54
AARG57
AHOH246
AHOH360

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 184
ChainResidue
AMET137
AASN138
ACYS139
AARG142
BARG107
BHOH264

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 185
ChainResidue
AARG107
AASP144
BARG142
BHOH309

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 186
ChainResidue
ASER162
ASER163
AGLN164
AHOH201
AHOH477

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 182
ChainResidue
BILE12
BSER77
BMET78
BHOH314

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 183
ChainResidue
BTRP42
BARG57
BHOH240

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 184
ChainResidue
BSER162
BSER163
BGLN164
BHOH371

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 185
ChainResidue
BILE135
BHOH209

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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