Structure of PDB 1isp Chain A

Receptor sequence
>1ispA (length=179) Species: 1423 (Bacillus subtilis) [Search protein sequence]
EHNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNN
GPVLSRFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVT
LGGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQI
HGVGHIGLLYSSQVNSLIKEGLNGGGQNT
3D structure
PDB1isp Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) I12 S77 M78 D133 H156
Catalytic site (residue number reindexed from 1) I11 S76 M77 D132 H155
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 GOL A G11 I12 G14 N18 H76 G10 I11 G13 N17 H75
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1isp, PDBe:1isp, PDBj:1isp
PDBsum1isp
PubMed12077437
UniProtP37957|ESTA_BACSU Lipase EstA (Gene Name=estA)

[Back to BioLiP]