GL1X · GenesisL1 explorer

Research workbench

Structure of lipase tl from bulk agarose grown crystal

Analyse Structure of lipase tl from bulk agarose grown crystal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7APN
Type
protein
Length
538 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lipase
EC
3.1.1.3
UniProt
O59952
Ligands
NAG, MG, PO4
Pockets
6 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLipase (EC 3.1.1.3)protein26933% helix, 25% strandO59952

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • PO4 · Phosphate ion · ion · 2 copies · chains A
  • GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12490.600.7940empty
2500.510.8817empty
3650.440.8318empty
41040.380.7519empty
51050.370.7521empty

Interfaces

1 interface between chains.

  • A–B · 591 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 7APN · Structure of Lipase TL from bulk agarose grown crystal · the same entry in another collection · chain A against A, TM-score 1.00
  • O59952 · AlphaFold monomer V2.0 prediction for lipase (O59952) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.