Structure of PDB 5cta Chain A

Receptor sequence
>5ctaA (length=179) Species: 1423 (Bacillus subtilis) [Search protein sequence]
HNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDETGTNENNG
PVLSEFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTL
GGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQIH
GVGHIELLYSSQVNSLIKEGLNGGGQNTN
3D structure
PDB5cta Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure.
ChainA
Resolution1.24 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) 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 BM0 A D34 L36 Y37 K61 D32 L34 Y35 K59
BS02 CL A M134 H156 M132 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5cta, PDBe:5cta, PDBj:5cta
PDBsum5cta
PubMed26388426
UniProtP37957|ESTA_BACSU Lipase EstA (Gene Name=estA)

[Back to BioLiP]