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Crystal structure of the catalytic domain of human tyrosine phosphatase receptor, type R
Analyse Crystal structure of the catalytic domain of human tyrosine phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A8B
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase R
- EC
- 3.1.3.48
- UniProt
- Q15256
- Ligands
- CL
- Pockets
- 4 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase R (EC 3.1.3.48) | protein | 283 | 38% helix, 22% strand | Q15256 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.50 | 0.79 | 23 | empty |
| 2 | 63 | 0.37 | 0.78 | 15 | empty |
| 3 | 71 | 0.35 | 0.77 | 21 | empty |
| 4 | 54 | 0.26 | 0.73 | 17 | empty |
Compared structures
- 2A8B · Crystal Structure of the Catalytic Domain of Human Tyrosine Phosphatase Receptor, Type R · the same entry in another collection · chain A against A, TM-score 1.00
- Q15256 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase R… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q15256
- Elsewhere: RCSB PDB 2A8B · PDBe 2A8B · UniProt Q15256
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