Research workbench
Affimer K6 - KRAS protein complex
Analyse Affimer K6 - KRAS protein complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YR8
- Type
- protein
- Length
- 253 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase KRAS; Affimer K6
- UniProt
- P01116
- Ligands
- GDP, MG
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase KRAS | protein | 164 | 37% helix, 26% strand | P01116 |
| B | Affimer K6 | protein | 89 | 20% helix, 62% strand | — |
Ligands and binding sites
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 | 120 | 0.44 | 0.77 | 26 | GDP, MG |
Interfaces
1 interface between chains.
- A–B · 531 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6YR8 · Affimer K6 - KRAS protein 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 P01116
- Elsewhere: RCSB PDB 6YR8 · PDBe 6YR8 · UniProt P01116
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