MolNFT v1 · #70377 · protein

Open conformation of pseudomonas cepacia lipase

3LIP · Triacyl-glycerol-hydrolase: “Open conformation of pseudomonas cepacia lipase”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.66). MolNFT v1 #70377 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3LIP
Type: protein
Length: 320 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Triacyl-glycerol-hydrolase
EC: 3.1.1.3
UniProt: P22088
Ligands: CA
Pockets: 1 · best druggability 0.66

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Triacyl-glycerol-hydrolase (EC 3.1.1.3)	protein	320	38% helix, 19% strand	P22088

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	407	0.66	0.78	37	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3LIP · Open conformation of pseudomonas cepacia 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 3LIP · PDBe 3LIP · UniProt P22088

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