MolNFT v1 · #22415 · protein

Allosteric inhibition of protein tyrosine phosphatase 1B

1T4J · Protein-tyrosine phosphatase, non-receptor type 1: “Allosteric inhibition of protein tyrosine phosphatase 1B”. X-ray diffraction, 1 ligand (FRJ), 1 pocket (best druggability 0.43). MolNFT v1 #22415 on GenesisL1: 3D structure…

PDB: 1T4J
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: FRJ
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 36% 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	36% helix, 23% strand	P18031

Ligands and binding sites

FRJ · 3-(3,5-dibromo-4-hydroxy-benzoyl)-2-ethyl-benzofuran-6-sulfonic acid [4-(thiazol-2-ylsulfamoyl)-phenyl]-amide · 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	116	0.43	0.77	20	empty

Compared structures

1T4J · 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 1T4J · PDBe 1T4J · UniProt P18031

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