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Notum Inhibitor ARUK3004552

Analyse Notum Inhibitor ARUK3004552 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8BTH
Type: protein
Length: 356 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.3
Source: Homo sapiens
Molecule: Palmitoleoyl-protein carboxylesterase NOTUM
EC: 3.1.1.98
UniProt: Q6P988
Ligands: RJ0, NAG, SO4
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · resolution 1.3 · 1 distinct chain · 33% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Palmitoleoyl-protein carboxylesterase NOTUM (EC 3.1.1.98)	protein	356	33% helix, 18% strand	Q6P988

Ligands and binding sites

RJ0 · 1-(2,3-dihydroindol-1-yl)prop-2-en-1-one · ligand · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A
DMS · Dimethyl sulfoxide · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	78	0.70	0.94	17	RJ0
2	136	0.43	0.76	19	empty

Modifications

Observed in the structure: 7 disulfide, 1 glycan (disulfide, N-glycosylation).

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 Q6P988
Elsewhere: RCSB PDB 8BTH · PDBe 8BTH · UniProt Q6P988

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