MolNFT v1 · #167397 · protein
Crystal structure of wild-type KRAS4B (gmppnp-bound) in complex with RAS-binding domain (rbd) of RAF1/CRAF
6VJJ: “Crystal structure of wild-type KRAS4B (gmppnp-bound) in complex with RAS-binding domain (rbd) of RAF1/CRAF”. X-ray diffraction, 3 ligands (GNP, MG, CL). MolNFT v1 #167397 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6VJJ
- Type
- protein
- Length
- 245 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01116, P04049
- Ligands
- GNP, MG, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 168 | — | P01116 |
| B | — | protein | 77 | — | P04049 |
Ligands and binding sites
- GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VJJ · Crystal Structure of wild-type KRAS4b (GMPPNP-bound) in complex with RAS-binding domain… · the same entry in another collection · chain A against A, TM-score 1.00
- P04049 · AlphaFold monomer V2.0 prediction for RAF proto-oncogene SERINE/THREONINE-protein kinase… · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P04049
- Elsewhere: RCSB PDB 6VJJ · PDBe 6VJJ · UniProt P01116 · UniProt P04049
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.