Structure of PDB 1lbt Chain A

Receptor sequence
>1lbtA (length=317) [Search protein sequence]
LPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDS
NWIPLSTQLGYTPCWISPPPFMLNDTQVNTEYMVNAITALYAGSGNNKLP
VLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVS
APSVWQQTTGSALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLD
SSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSALRSTTGQARS
ADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPY
ARPFAVGKRTCSGIVTP
3D structure
PDB1lbt Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols.
ChainA
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.1.3: triacylglycerol lipase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 T80 A T40 S105 Q106 L140 Q157 E188 I189 H224 A282 I285 T40 S105 Q106 L140 Q157 E188 I189 H224 A282 I285
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0016787 hydrolase activity
Biological Process
GO:0016042 lipid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1lbt, PDBe:1lbt, PDBj:1lbt
PDBsum1lbt
PubMed8527460
UniProtP41365|LIPB_PSEA2 Lipase B

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