MolNFT v1 · #166855 · protein
Crystal structure of the BRAF:MEK1 kinases in complex with amppnp
6V2W: “Crystal structure of the BRAF:MEK1 kinases in complex with amppnp”. X-ray diffraction, 2 ligands (ANP, MG). MolNFT v1 #166855 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6V2W
- Type
- protein
- Length
- 587 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P15056, Q02750
- Ligands
- ANP, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 275 | — | P15056 |
| B | — | protein | 312 | — | Q02750 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6V2W · Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP · the same entry in another collection · chain A against A, TM-score 1.00
- P15056 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase B-RAF (P15056) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 6V2W · PDBe 6V2W · UniProt P15056 · UniProt Q02750
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