Research workbench
RAS G12V - pi 3-kinase gamma complex
Analyse RAS G12V - pi 3-kinase gamma complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HE8
- Type
- protein
- Length
- 915 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3-kinase catalytic subunit, gamma isoform; Transforming protein…
- EC
- 2.7.1.137
- UniProt
- P48736, P23175
- Ligands
- GNP, MG
- Pockets
- 14 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 3-kinase catalytic subunit, gamma isoform (EC 2.7.1.137) | protein | 749 | 42% helix, 18% strand | P48736 |
| B | Transforming protein P21/H-RAS-1 | protein | 166 | 39% helix, 24% strand | P23175 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains B
- MG · Magnesium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1071 | 0.83 | 0.84 | 78 | empty |
| 2 | 99 | 0.75 | 0.96 | 34 | empty |
| 3 | 291 | 0.64 | 0.80 | 31 | empty |
| 4 | 358 | 0.62 | 0.78 | 36 | empty |
| 5 | 228 | 0.60 | 0.80 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 733 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1HE8 · Ras G12V - PI 3-kinase gamma complex · the same entry in another collection · chain A against A, TM-score 1.00
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 P48736
- Every structure of UniProt P23175
- Elsewhere: RCSB PDB 1HE8 · PDBe 1HE8 · UniProt P48736 · UniProt P23175
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