MolNFT v1 · #94735 · protein
PP2A PR70 holoenzyme MODEL3_DICA_RCSB.PDB BPPNAT5_EXTEND.MTZ
4I5K · SERINE/THREONINE-protein phosphatase 2A regulatory subunit…: “PP2A PR70 holoenzyme MODEL3_DICA_RCSB.PDB BPPNAT5_EXTEND.MTZ”. X-ray diffraction, 1 ligand (CA), 7 pockets (best druggability 0.68). MolNFT v1 #94735 on GenesisL1: 3D…
- PDB
- 4I5K
- Type
- protein
- Length
- 532 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein phosphatase 2A regulatory subunit B'' subunit alpha
- UniProt
- Q06190
- Ligands
- CA
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SERINE/THREONINE-protein phosphatase 2A regulatory subunit B'' subunit alpha | protein | 266 | 59% helix, 5% strand | Q06190 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 513 | 0.68 | 0.78 | 50 | empty |
| 2 | 387 | 0.57 | 0.75 | 35 | empty |
| 3 | 157 | 0.53 | 0.80 | 24 | empty |
| 4 | 112 | 0.49 | 0.80 | 19 | empty |
| 5 | 190 | 0.46 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 571 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4I5K · PP2A PR70 Holoenzyme model3_diCa_rcsb.pdb bppnat5_extend.mtz · the same entry in another collection · chain A against A, TM-score 1.00
- Q06190 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 2A regulatory… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q06190
- Elsewhere: RCSB PDB 4I5K · PDBe 4I5K · UniProt Q06190
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