Research workbench
Crystal structure of P110ALPHA H1047R mutant in complex with NISH2 of P85ALPHA
Analyse Crystal structure of P110ALPHA H1047R mutant in complex with NISH2 of P85ALPHA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HIZ
- Type
- protein
- Length
- 1,258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform…
- EC
- 2.7.1.153
- UniProt
- P42336, P27986
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (EC 2.7.1.153) | protein | 1024 | 37% helix, 15% strand | P42336 |
| B | Phosphatidylinositol 3-kinase regulatory subunit alpha | protein | 234 | 53% helix, 9% strand | P27986 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1121 | 0.86 | 0.86 | 102 | empty |
| 2 | 464 | 0.81 | 0.88 | 56 | empty |
| 3 | 384 | 0.80 | 0.89 | 50 | empty |
| 4 | 291 | 0.78 | 0.90 | 56 | empty |
| 5 | 91 | 0.66 | 0.91 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 3137 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 3HIZ · Crystal structure of p110alpha H1047R mutant in complex with niSH2 of p85alpha · the same entry in another collection · chain A against A, TM-score 1.00
- P42336 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4,5-bisphosphate 3-kinase… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P42336
- Every structure of UniProt P27986
- Elsewhere: RCSB PDB 3HIZ · PDBe 3HIZ · UniProt P42336 · UniProt P27986
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