Research workbench
BRAF in complex with compound 3
Analyse BRAF in complex with compound 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H58
- Type
- protein
- Length
- 797 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.1
- Source
- Homo sapiens
- Molecule
- Serine/threonine-protein kinase B-raf
- EC
- 2.7.11.1
- UniProt
- P15056
- Ligands
- 10Z, CL
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · resolution 3.1 · 3 distinct chains · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine/threonine-protein kinase B-raf (EC 2.7.11.1) | protein | 263 | 40% helix, 17% strand | P15056 |
| B | Serine/threonine-protein kinase B-raf (EC 2.7.11.1) | protein | 262 | 39% helix, 15% strand | P15056 |
| C | Serine/threonine-protein kinase B-raf (EC 2.7.11.1) | protein | 272 | 38% helix, 15% strand | P15056 |
Ligands and binding sites
- 10Z · N-(4-{[(2-methoxyethyl)amino]methyl}phenyl)-6-(pyridin-4-yl)quinazolin-2-amine · ligand · chains A
- CL · Chloride ion · ion · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 549 | 0.74 | 0.82 | 69 | CL |
| 2 | 337 | 0.71 | 0.83 | 36 | empty |
| 3 | 247 | 0.66 | 0.83 | 30 | 10Z |
| 4 | 454 | 0.64 | 0.77 | 61 | empty |
| 5 | 70 | 0.62 | 0.91 | 21 | empty |
Interfaces
2 interfaces between chains.
- A–C · 1147 Ų buried · 19 hydrogen bonds · protein-protein
- B–C · 284 Ų buried · 0 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 P15056
- Elsewhere: RCSB PDB 4H58 · PDBe 4H58 · UniProt P15056
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