Research workbench

Protein Tyrosine Phosphatase 1B P185G mutant, open state

Analyse Protein Tyrosine Phosphatase 1B P185G mutant, open state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KAC
Type: protein
Length: 279 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.9
Source: Homo sapiens
Molecule: Tyrosine-protein phosphatase non-receptor type 1
EC: 3.1.3.48
UniProt: P18031
Ligands: CL
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · resolution 1.9 · 1 distinct chain · 34% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48)	protein	279	34% helix, 23% strand	P18031

Ligands and binding sites

CL · Chloride ion · ion · 7 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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	77	0.36	0.77	19	CL, GOL

Compared structures

5KAC · Protein tyrosine phosphatase 1B P185G mutant, open state · 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 5KAC · PDBe 5KAC · UniProt P18031

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