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Structure of lipase

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

PDB: 1OIL
Type: protein
Length: 640 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.1
Source: Burkholderia cepacia
Molecule: Lipase
EC: 3.1.1.3
UniProt: P22088
Ligands: CA
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · resolution 2.1 · 1 distinct chain · 38% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase (EC 3.1.1.3)	protein	320	38% helix, 19% strand	P22088

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	449	0.66	0.78	37	empty
2	422	0.64	0.77	39	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1OIL · Structure of lipase · the same entry in another collection · chain A against A, TM-score 1.00
P22088 · AlphaFold monomer V2.0 prediction for triacylglycerol lipase (P22088) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P22088
Elsewhere: RCSB PDB 1OIL · PDBe 1OIL · UniProt P22088

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