Research workbench
Complex of RAS-GDP with RAFRBD(A85K)
Analyse Complex of RAS-GDP with RAFRBD(A85K) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KUD
- Type
- protein
- Length
- 241 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTPase HRAS; RAF proto-oncogene SERINE/THREONINE-protein kinase
- EC
- 2.7.11.1
- UniProt
- P01112, P04049
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTPase HRAS | protein | 165 | 31% helix, 26% strand | P01112 |
| B | RAF proto-oncogene SERINE/THREONINE-protein kinase (EC 2.7.11.1) | protein | 76 | 22% helix, 33% strand | P04049 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 286 | 0.68 | 0.83 | 48 | GDP, MG |
| 2 | 85 | 0.42 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 573 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
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 P01112
- Every structure of UniProt P04049
- Elsewhere: RCSB PDB 3KUD · PDBe 3KUD · UniProt P01112 · UniProt P04049
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