Research workbench

Potent, selective inhibitors of protein tyrosine phosphatase 1B using a second phosphotyrosine binding site, complexed with compound 19.

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

PDB: 1NZ7
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: 901
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 22% 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, 22% strand	P18031

Ligands and binding sites

901 · 2-[(4-{2-acetylamino-2-[4-(1-carboxy-3-methylsulfanyl-propylcarbamoyl)-butylcarbamoyl]-ethyl}-2-ethyl-phenyl)-oxalyl-am ino]-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	142	0.45	0.76	23	901

Compared structures

1NZ7 · POTENT, SELECTIVE INHIBITORS OF PROTEIN TYROSINE PHOSPHATASE 1B USING A SECOND… · 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 1NZ7 · PDBe 1NZ7 · UniProt P18031

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.