Structure of PDB 5ct6 Chain A

Receptor sequence
>5ct6A (length=179) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
HNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDKTGTNYNNG
PVLSRFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTL
GGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQIH
GVGHIGLLYSSQVNSLIKEGLNGGGQNTN
3D structure
PDB5ct6 Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure.
ChainA
Resolution1.902 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 CL A G155 I157 G153 I155
BS02 BM0 A I12 G13 G14 N18 S77 I10 G11 G12 N16 S75
BS03 BM0 A Y49 N50 Y47 N48
BS04 BM0 A G116 D118 P119 K122 G114 D116 P117 K120
BS05 BM0 A D34 L36 Y37 D32 L34 Y35
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ct6, PDBe:5ct6, PDBj:5ct6
PDBsum5ct6
PubMed26388426
UniProtP37957|ESTA_BACSU Lipase EstA (Gene Name=estA)

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