Research workbench
KRAS full length wild-type in complex with RGL1 RAS association domain
Analyse KRAS full length wild-type in complex with RGL1 RAS association domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SCW
- Type
- protein
- Length
- 257 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2B of GTPase KRAS; Ral guanine nucleotide dissociation stimulator-like 1
- EC
- 3.6.5.2
- UniProt
- P01116, Q9NZL6
- Ligands
- GSP, MG
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 2B of GTPase KRAS (EC 3.6.5.2) | protein | 171 | 40% helix, 25% strand | P01116 |
| B | Ral guanine nucleotide dissociation stimulator-like 1 | protein | 86 | 21% helix, 42% strand | Q9NZL6 |
Ligands and binding sites
- GSP · 5'-guanosine-diphosphate-monothiophosphate · 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
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 | 304 | 0.65 | 0.81 | 42 | MG, GSP |
| 2 | 63 | 0.34 | 0.77 | 12 | empty |
| 3 | 51 | 0.33 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 607 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 7SCW · KRAS full length wild-type in complex with RGL1 Ras association domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NZL6 · AlphaFold monomer V2.0 prediction for ral guanine nucleotide dissociation stimulator-like… · a predicted model of the same protein · chain B against A, TM-score 0.93
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
- Every structure of UniProt Q9NZL6
- Elsewhere: RCSB PDB 7SCW · PDBe 7SCW · UniProt P01116 · UniProt Q9NZL6
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