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Crystal structure of the human protein tyrosine phosphatase PTPN5 (step, striatum enriched enriched phosphatase)

Analyse Crystal structure of the human protein tyrosine phosphatase PTPN5 (step… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BIJ
Type: protein
Length: 284 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein phosphatase, non-receptor type 5
EC: 3.1.3.48
UniProt: P54829
Ligands: SO4
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein phosphatase, non-receptor type 5 (EC 3.1.3.48)	protein	284	39% helix, 21% strand	P54829

Ligands and binding sites

SO4 · Sulfate ion · ion · 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	92	0.42	0.78	18	empty

Compared structures

2BIJ · Crystal structure of the human protein tyrosine phosphatase PTPN5 (STEP, striatum… · the same entry in another collection · chain A against A, TM-score 1.00
P54829 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 5… · 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 P54829
Elsewhere: RCSB PDB 2BIJ · PDBe 2BIJ · UniProt P54829

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