MolNFT v1 · #33494 · protein

Structural basis for inhibition of protein tyrosine phosphatase 1B by isothiazolidinone heterocyclic phosphonate mimetics

2CMA · Tyrosine-protein phosphatase non-receptor type 1: “Structural basis for inhibition of protein tyrosine phosphatase 1B by isothiazolidinone heterocyclic…”. X-ray diffraction, 1 ligand (F20), 1 pocket (best druggability 0.45). MolNFT…

PDB: 2CMA
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein phosphatase non-receptor type 1
EC: 3.1.3.48
UniProt: P18031
Ligands: F20
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48)	protein	296	38% helix, 20% strand	P18031

Ligands and binding sites

F20 · N-benzoyl-L-phenylalanyl-4-[(5S)-1,1-dioxido-3-oxoisothiazolidin-5-yl]-L-phenylalaninamide · 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	115	0.45	0.78	26	F20

Compared structures

2CMA · Structural Basis for Inhibition of Protein Tyrosine Phosphatase 1B by Isothiazolidi… · 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 2CMA · PDBe 2CMA · UniProt P18031

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