Structure of PDB 1r4z Chain A

Receptor sequence
>1r4zA (length=179) Species: 1423 (Bacillus subtilis) [Search protein sequence]
HNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNNG
PVLSRFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTL
GGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQIH
GVGHIGLLYSSQVNSLIKEGLNGGGQNTN
3D structure
PDB1r4z Directed Evolution of Bacillus subtilis Lipase A by Use of Enantiomeric Phosphonate Inhibitors: Crystal Structures and Phage Display Selection
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I12 S77 M78 D133 H156
Catalytic site (residue number reindexed from 1) I10 S75 M76 D131 H154
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 RIL A G11 I12 G14 S77 M78 H156 G9 I10 G12 S75 M76 H154
Gene Ontology
Molecular Function
GO:0004806 triacylglycerol lipase activity
GO:0016298 lipase activity
GO:0016787 hydrolase activity
Biological Process
GO:0016042 lipid catabolic process
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:1r4z, PDBe:1r4z, PDBj:1r4z
PDBsum1r4z
PubMed16342303
UniProtP37957|ESTA_BACSU Lipase EstA (Gene Name=estA)

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