Research workbench

Truncated recombinant human bile salt stimulated lipase

Analyse Truncated recombinant human bile salt stimulated lipase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JMY
Type: protein
Length: 515 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile-salt-activated lipase
EC: 3.1.1.3
UniProt: P19835
Ligands: SO4
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bile-salt-activated lipase (EC 3.1.1.3)	protein	515	33% helix, 17% strand	P19835

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

4 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	355	0.63	0.78	38	empty
2	417	0.62	0.76	48	empty
3	87	0.48	0.82	17	empty
4	81	0.41	0.79	20	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1JMY · Truncated Recombinant Human Bile Salt Stimulated Lipase · the same entry in another collection · chain A against A, TM-score 1.00
P19835 · AlphaFold monomer V2.0 prediction for bile salt-activated lipase (P19835) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P19835
Elsewhere: RCSB PDB 1JMY · PDBe 1JMY · UniProt P19835

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