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Lipase (E.C.3.1.1.3) (triacylglycerol hydrolase)

Analyse Lipase (E.C.3.1.1.3) (triacylglycerol hydrolase) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1LBT
Type
protein
Length
634 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lipase B
EC
3.1.1.3
UniProt
P41365
Ligands
T80, NAG
Pockets
3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLipase B (EC 3.1.1.3)protein31738% helix, 15% strandP41365

Ligands and binding sites

  • T80 · Methylpenta(oxyethyl) heptadecanoate · ligand · 2 copies · chains A, B
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15870.670.7657empty
21620.610.8423T80
31550.610.8420T80

Interfaces

1 interface between chains.

  • A–B · 317 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 1LBT · Lipase (E.C.3.1.1.3) (triacylglycerol hydrolase) · the same entry in another collection · chain A against A, TM-score 1.00
  • P41365 · AlphaFold monomer V2.0 prediction for lipase B (P41365) · a predicted model of the same protein · chain A against A, TM-score 1.00

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