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Allosteric inhibition of protein tyrosine phosphatase 1B

Analyse Allosteric inhibition of protein tyrosine phosphatase 1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T49
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: 892, MG
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-tyrosine phosphatase, non-receptor type 1 (EC 3.1.3.48)	protein	282	38% helix, 23% strand	P18031

Ligands and binding sites

892 · 3-(3,5-dibromo-4-hydroxy-benzoyl)-2-ethyl-benzofuran-6-sulfonic acid (4-sulfamoyl-phenyl)-amide · ligand · chains A
MG · Magnesium 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	128	0.45	0.77	23	empty

Compared structures

1T49 · Allosteric Inhibition of Protein Tyrosine Phosphatase 1B · 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 1T49 · PDBe 1T49 · UniProt P18031

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