MolNFT v1 · #38494 · protein

Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors

2H03 · Protein tyrosine phosphatase, receptor type, B,: “Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors”. X-ray diffraction, 3 ligands (3UN, MG, CL), 2 pockets (best druggability 0.37).…

PDB: 2H03
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein tyrosine phosphatase, receptor type, B,
EC: 3.1.3.48
UniProt: Q3MIV7
Ligands: 3UN, MG, CL
Pockets: 2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein tyrosine phosphatase, receptor type, B, (EC 3.1.3.48)	protein	288	38% helix, 23% strand	Q3MIV7

Ligands and binding sites

3UN · (4-{4-[(tert-butoxycarbonyl)amino]-2,2-bis(ethoxycarbonyl)butyl}phenyl)sulfamic acid · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 2 copies · 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	53	0.37	0.80	15	3UN
2	73	0.32	0.75	21	CL

Compared structures

2H03 · Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with… · 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 Q3MIV7
Elsewhere: RCSB PDB 2H03 · PDBe 2H03 · UniProt Q3MIV7

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