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Potent, selective protein tyrosine phosphatase 1B inhibitor compound 12 using a linked-fragment strategy

Analyse Potent, selective protein tyrosine phosphatase 1B inhibitor compound 12 using a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NL9
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: 989
Pockets: 1 · best druggability 0.47

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

989 · 2-{[4-(2-acetylamino-2-pentylcarbamoyl-ethyl)-naphthalen-1-yl]-oxalyl-amino}-benzoic 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	165	0.47	0.76	23	989

Compared structures

1NL9 · Potent, Selective Protein Tyrosine Phosphatase 1B Inhibitor Compound 12 Using a… · 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 1NL9 · PDBe 1NL9 · UniProt P18031

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