Research workbench
Human KRAS in complex with darpin K13
Analyse Human KRAS in complex with darpin K13 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H46
- Type
- protein
- Length
- 324 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase KRAS; Darpin K13
- UniProt
- P01116
- Ligands
- GDP, SO4
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase KRAS | protein | 168 | 39% helix, 23% strand | P01116 |
| B | Darpin K13 | protein | 156 | 55% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 172 | 0.57 | 0.81 | 29 | empty |
| 2 | 60 | 0.32 | 0.76 | 18 | empty |
| 3 | 53 | 0.27 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1046 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6H46 · Human KRAS in complex with darpin K13 · 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 6H46 · PDBe 6H46 · UniProt P01116
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