Research workbench
Crystal structure of the phosphotyrosyl phosphatase activator
Analyse Crystal structure of the phosphotyrosyl phosphatase activator in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HV6
- Type
- protein
- Length
- 596 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein phosphatase 2A, regulatory subunit B
- UniProt
- Q15257
- Ligands
- MG
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 60% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein phosphatase 2A, regulatory subunit B | protein | 301 | 61% helix, 4% strand | Q15257 |
| B | Protein phosphatase 2A, regulatory subunit B | protein | 295 | 59% helix, 4% strand | Q15257 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1189 | 0.79 | 0.80 | 88 | empty |
| 2 | 134 | 0.52 | 0.80 | 27 | empty |
| 3 | 70 | 0.38 | 0.78 | 13 | empty |
| 4 | 96 | 0.37 | 0.76 | 19 | empty |
| 5 | 59 | 0.33 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 761 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2HV6 · Crystal structure of the phosphotyrosyl phosphatase activator · the same entry in another collection · chain A against A, TM-score 1.00
- Q15257 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 2A activator… · 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 Q15257
- Elsewhere: RCSB PDB 2HV6 · PDBe 2HV6 · UniProt Q15257
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