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Structural studies of protein tyrosine phosphatase beta catalytic domain in complex with inhibitors
Analyse Structural studies of protein tyrosine phosphatase beta catalytic domain in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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.
| Volume (ų) | 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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