MolNFT v1 · #75479 · protein
Crystal structure of human B-RAF kinase in complex with a non-oxime furopyridine inhibitor
3PRI · SERINE/THREONINE-protein kinase B-RAF: “Crystal structure of human B-RAF kinase in complex with a non-oxime furopyridine inhibitor”. X-ray diffraction, 1 ligand (FP4), 3 pockets (best druggability 0.70). MolNFT v1 #75479 on…
- PDB
- 3PRI
- Type
- protein
- Length
- 528 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase B-RAF
- EC
- 2.7.11.1
- UniProt
- P15056
- Ligands
- FP4
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SERINE/THREONINE-protein kinase B-RAF (EC 2.7.11.1) | protein | 264 | 36% helix, 17% strand | P15056 |
Ligands and binding sites
- FP4 · 3-(4-{[2-(pyrimidin-2-yl)furo[2,3-c]pyridin-3-yl]amino}-1H-indazol-3-yl)propan-1-ol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 376 | 0.70 | 0.82 | 45 | FP4 |
| 2 | 347 | 0.69 | 0.82 | 45 | FP4 |
| 3 | 437 | 0.69 | 0.81 | 49 | empty |
Interfaces
1 interface between chains.
- A–B · 1152 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3PRI · Crystal Structure of Human B-Raf Kinase in Complex with a Non-Oxime Furopyridine Inhibitor · 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 B 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
- Elsewhere: RCSB PDB 3PRI · PDBe 3PRI · UniProt P15056
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