Structure of PDB 1ex9 Chain A

Receptor sequence

>1ex9A (length=285) Species: 287 (Pseudomonas aeruginosa)

STYTQTKYPIVLAHGMLGFDNILGVDYWFGIPSALRRDGAQVYVTEVSQL
DTSEVRGEQLLQQVEEIVALSGQPKVNLIGHSHGGPTIRYVAAVRPDLIA
SATSVGAPHKGSDTADFLRQIPPGSAGEAVLSGLVNSLGALISFLSSGST
GTQNSLGSLESLNSEGAARFNAKYPQGIPTSACGEGAYKVNGVSYYSWSG
SSPLTNFLDPSDAFLGASSLTFKNGTANDGLVGTCSSHLGMVIRDNYRMN
HLDEVNQVFGLTSLFETSPVSVYRQHANRLKNASL

3D structure

• PDB: 1ex9 Crystal structure of pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases.
• Chain: A
• Resolution: 2.54 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): M16 S82 H83 D209 D229 H251 D253 Q257 L261
• Catalytic site (residue number reindexed from 1): M16 S82 H83 D209 D229 H251 D253 Q257 L261
• 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	CA	A	D209 D253 Q257 L261	D209 D253 Q257 L261
BS02	OCP	A	G15 M16 L17 S82 H83 S112 H251	G15 M16 L17 S82 H83 S112 H251

Gene Ontology

Molecular Function

• GO:0004806 triacylglycerol lipase activity
• GO:0016298 lipase activity
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0015628 protein secretion by the type II secretion system
• GO:0016042 lipid catabolic process
• GO:0043952 protein transport by the Sec complex

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:1ex9, PDBe:1ex9, PDBj:1ex9
• PDBsum: 1ex9
• PubMed: 10893416
• UniProt: P26876|LIP_PSEAE Triacylglycerol lipase (Gene Name=lip)