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Crystal structure of protein tyrosine phosphatase 1B in complex with an isothiazolidinone-containing inhibitor

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

PDB: 2VEU
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: IZ1
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 35% 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	35% helix, 20% strand	P18031

Ligands and binding sites

IZ1 · N-[(1S)-2-{4-[(5S)-1,1-dioxido-3-oxoisothiazolidin-5-yl]phenyl}-1-(4-phenyl-1H-imidazol-2-yl)ethyl]-3-(trifluoromethyl)benzenesulfonamide · 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	52	0.42	0.83	15	empty

Compared structures

2VEU · Crystal structure of protein tyrosine phosphatase 1B in complex with an 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 2VEU · PDBe 2VEU · UniProt P18031

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