Structure of PDB 5cur Chain A

Receptor sequence
>5curA (length=179) Species: 1423 (Bacillus subtilis) [Search protein sequence]
HNPVVMVHGIGGASFNFAGIKSYLVSQGWSRDKLYAVDFWDETGTNENNG
PVLSEFVQKVLDETGAKKVDIVAHSMGGANTLYYIKNLDGGNKVANVVTL
GGANRLTTGKALPGTDPNQKILYTSIYSSADMIVMNYLSRLDGARNVQIH
GVGHIELLYSSQVNSLIKEGLNGGGQNTN
3D structure
PDB5cur Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure.
ChainA
Resolution1.302 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 BM0 A Y37 F58 K61 E65 Y35 F56 K59 E63
BS02 BM0 A A20 G21 Y161 A18 G19 Y159
BS03 BM0 A I12 G13 N18 H76 S77 H156 I157 I10 G11 N16 H74 S75 H154 I155
BS04 BM0 A H3 G30 W31 N174 H1 G28 W29 N172
BS05 CL A M134 H156 M132 H154
BS06 CL A H10 G11 N18 H76 H8 G9 N16 H74
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:5cur, PDBe:5cur, PDBj:5cur
PDBsum5cur
PubMed26388426
UniProtP37957|ESTA_BACSU Lipase EstA (Gene Name=estA)

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