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Crystal structure of the catalytic domain of protein tyrosine phosphatase PTP-SL/BR7

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

PDB: 1JLN
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.81
Source: Mus musculus
Molecule: Protein Tyrosine Phosphatase, receptor type, R
EC: 3.1.3.48
UniProt: Q62132
Pockets: 3 · best druggability 0.46

Structure

x-ray diffraction · resolution 1.81 · 1 distinct chain · 38% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein Tyrosine Phosphatase, receptor type, R (EC 3.1.3.48)	protein	297	38% helix, 19% strand	Q62132

Pockets

3 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	161	0.46	0.75	23	empty
2	86	0.39	0.77	20	empty
3	66	0.37	0.78	14	empty

Compared structures

1JLN · Crystal structure of the catalytic domain of protein tyrosine phosphatase ptp-SL/BR7 · the same entry in another collection · chain A against A, TM-score 1.00
Q62132 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase R… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q62132
Elsewhere: RCSB PDB 1JLN · PDBe 1JLN · UniProt Q62132

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