Research workbench
Crystal structure of BRAF:MEK1 complex
Analyse Crystal structure of BRAF:MEK1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PP9
- Type
- protein
- Length
- 590 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15056, Q02750
- Ligands
- ANP, LCJ, MG, CL, SO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 276 | — | P15056 |
| B | — | protein | 314 | — | Q02750 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- LCJ · 5-[(2-fluoro-4-iodophenyl)amino]-N-(2-hydroxyethoxy) imidazo[1,5-a]pyridine-6-carboxamide · ligand · chains B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies
- SO4 · Sulfate ion · ion · chains B
- GOL · Glycerol · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P15056
- Every structure of UniProt Q02750
- Elsewhere: RCSB PDB 6PP9 · PDBe 6PP9 · UniProt P15056 · UniProt Q02750
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.