MolNFT v1 · #38874 · protein

Engineered catalytic domain of protein tyrosine phosphatase hptpbeta.

2HC1 · Receptor-type tyrosine-protein phosphatase beta: “Engineered catalytic domain of protein tyrosine phosphatase hptpbeta.”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.50). MolNFT v1 #38874 on GenesisL1: 3D…

PDB: 2HC1
Type: protein
Length: 290 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: CL
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Receptor-type tyrosine-protein phosphatase beta (EC 3.1.3.48)	protein	290	36% helix, 21% strand	P23467

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	156	0.50	0.78	22	empty
2	84	0.31	0.73	19	CL

Compared structures

2HC1 · Engineered catalytic domain of protein tyrosine phosphatase HPTPbeta. · 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 0.96

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 2HC1 · PDBe 2HC1 · UniProt P23467

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