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Structure-based design of protein tyrosine phosphatase-1B inhibitors

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

PDB: 2BGD
Type: protein
Length: 294 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: T1D, NA, CL, PO4
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein-tyrosine phosphatase non-receptor type 1 (EC 3.1.3.48)	protein	294	37% helix, 21% strand	P18031

Ligands and binding sites

T1D · 5-(4-methoxybiphenyl-3-yl)-1,2,5-thiadiazolidin-3-one 1,1-dioxide · ligand · chains A
NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · 3 copies · chains A
PO4 · Phosphate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.49	0.83	15	T1D
2	50	0.22	0.71	12	empty

Compared structures

2BGD · Structure-based design of Protein Tyrosine Phosphatase-1B Inhibitors · the same entry in another collection · chain A against A, TM-score 1.00

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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 2BGD · PDBe 2BGD · UniProt P18031

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