MolNFT v1 · #90661 · protein
Discovery of small molecules that bind to K-RAS and inhibit sos- mediated activation
4EPY · GTPase KRAS: “Discovery of small molecules that bind to K-RAS and inhibit sos- mediated activation”. X-ray diffraction, 3 ligands (GDP, 0QY, MG), 1 pocket (best druggability 0.54). MolNFT v1 #90661 on GenesisL1: 3D structure…
- PDB
- 4EPY
- Type
- protein
- Length
- 170 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase KRAS
- EC
- 3.6.5.2
- UniProt
- P01116
- Ligands
- GDP, 0QY, MG
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase KRAS (EC 3.6.5.2) | protein | 170 | 38% helix, 24% strand | P01116 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- 0QY · N-[2-(1H-indol-3-ylmethyl)-1H-benzimidazol-5-yl]-L-prolinamide · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.54 | 0.79 | 39 | GDP, MG |
Compared structures
- 4EPY · Discovery of Small Molecules that Bind to K-Ras and Inhibit Sos-mediated Activation · 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 P01116
- Elsewhere: RCSB PDB 4EPY · PDBe 4EPY · UniProt P01116
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