MolNFT v1 · #166936 · protein
The haddock structure model of GDP KRAS in complex with its allosteric inhibitor E22
6V5L · GTPase KRAS: “The haddock structure model of GDP KRAS in complex with its allosteric inhibitor E22”. Solution nmr, 3 ligands (GDP, QPD, MG), 1 pocket (best druggability 0.45). MolNFT v1 #166936 on GenesisL1: 3D structure, binding…
- PDB
- 6V5L
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase KRAS
- UniProt
- P01116
- Ligands
- GDP, QPD, MG
- Pockets
- 1 · best druggability 0.45
Structure
solution nmr · 1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase KRAS | protein | 169 | 38% helix, 25% strand | P01116 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- QPD · (2R)-2-[2-(1H-indole-3-carbonyl)hydrazinyl]-2-phenylacetamide · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.45 | 0.77 | 25 | GDP |
Compared structures
- 6V5L · The HADDOCK structure model of GDP KRas in complex with its allosteric inhibitor E22 · 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 6V5L · PDBe 6V5L · UniProt P01116
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