Research workbench
Crystal structure of the catalytic domain of protein tyrosine phosphatase from homo sapiens
Analyse Crystal structure of the catalytic domain of protein tyrosine phosphatase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G59
- Type
- protein
- Length
- 569 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase O
- EC
- 3.1.3.48
- UniProt
- Q16827
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase O (EC 3.1.3.48) | protein | 287 | 38% helix, 20% strand | Q16827 |
| B | Receptor-type tyrosine-protein phosphatase O (EC 3.1.3.48) | protein | 282 | 40% helix, 20% strand | Q16827 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 700 | 0.86 | 0.89 | 50 | empty |
| 2 | 267 | 0.65 | 0.82 | 40 | empty |
| 3 | 154 | 0.46 | 0.76 | 23 | empty |
| 4 | 105 | 0.38 | 0.75 | 24 | empty |
| 5 | 54 | 0.33 | 0.77 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 677 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2G59 · Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase from Homo… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16827 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase O… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q16827
- Elsewhere: RCSB PDB 2G59 · PDBe 2G59 · UniProt Q16827
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