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1ISP

Crystal structure of Bacillus subtilis lipase at 1.3A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004806molecular_functiontriacylglycerol lipase activity
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 200
ChainResidue
AGLY11
AHOH417
AILE12
AGLY14
AASN18
AHIS76
ASER77
AILE157
ALEU160
AHOH316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive 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"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1r4z
ChainResidueDetails
AASP133
AHIS156
AMET78
ASER77
AILE12

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

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PDB entries from 2025-08-06

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