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Engineered protein tyrosine phosphatase beta catalytic domain

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

PDB: 2HC2
Type: protein
Length: 284 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Receptor-type tyrosine-protein phosphatase beta
EC: 3.1.3.48
UniProt: P23467
Ligands: NA, MG
Pockets: 2 · best druggability 0.43

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Receptor-type tyrosine-protein phosphatase beta (EC 3.1.3.48)	protein	284	37% helix, 21% strand	P23467

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A
MG · Magnesium ion · metal · 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	142	0.43	0.75	23	NA
2	64	0.36	0.78	16	empty

Compared structures

2HC2 · Engineered protein tyrosine phosphatase beta catalytic domain · the same entry in another collection · chain A against A, TM-score 1.00
P23467 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase beta… · 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 P23467
Elsewhere: RCSB PDB 2HC2 · PDBe 2HC2 · UniProt P23467

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