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Dual-site potent, selective protein tyrosine phosphatase 1B inhibitor using a linked fragment strategy and a malonate head on the first site

Analyse Dual-site potent, selective protein tyrosine phosphatase 1B inhibitor using a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PYN
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein-tyrosine phosphatase, non-receptor type 1
EC: 3.1.3.48
UniProt: P18031
Ligands: 941
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-tyrosine phosphatase, non-receptor type 1 (EC 3.1.3.48)	protein	282	37% helix, 21% strand	P18031

Ligands and binding sites

941 · 2-(4-{2-tert-butoxycarbonylamino-2-[4-(3-hydroxy-2-methoxycarbonyl-phenoxy)-butylcarbamoyl]-ethyl}-phenoxy)-malonic acid · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	145	0.46	0.77	22	empty

Compared structures

1PYN · Dual-site potent, selective protein tyrosine phosphatase 1B inhibitor using a linked… · the same entry in another collection · chain A against A, TM-score 1.00

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 P18031
Elsewhere: RCSB PDB 1PYN · PDBe 1PYN · UniProt P18031

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