Structure of PDB 1lbs Chain E

Receptor sequence
>1lbsE (length=317) [Search protein sequence]
LPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDS
NWIPLSTQLGYTPCWISPPPFMLNDTQVNTEYMVNAITALYAGSGNNKLP
VLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVS
APSVWQQTTGSALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLD
SSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFSYVVGRSALRSTTGQARS
ADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPY
ARPFAVGKRTCSGIVTP
3D structure
PDB1lbs Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols.
ChainE
Resolution2.6 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 HEE E G39 T40 S105 Q106 D134 I189 H224 L278 G39 T40 S105 Q106 D134 I189 H224 L278
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:1lbs, PDBe:1lbs, PDBj:1lbs
PDBsum1lbs
PubMed8527460
UniProtP41365|LIPB_PSEA2 Lipase B

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