Research workbench
Crystal structure of the BRAF:MEK1 complex
Analyse Crystal structure of the 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
- 4MNE
- Type
- protein
- Length
- 2,179 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dual specificity mitogen-activated protein kinase kinase 1; SERINE/THREONINE-protein…
- EC
- 2.7.12.2, 2.7.11.1
- UniProt
- Q02750, P15056
- Ligands
- 573, ACP, MG, CL
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 8 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dual specificity mitogen-activated protein kinase kinase 1 (EC 2.7.12.2) | protein | 286 | 45% helix, 17% strand | Q02750 |
| B | SERINE/THREONINE-protein kinase B-RAF (EC 2.7.11.1) | protein | 270 | 39% helix, 14% strand | P15056 |
| C | SERINE/THREONINE-protein kinase B-RAF (EC 2.7.11.1) | protein | 260 | 41% helix, 18% strand | P15056 |
| D | Dual specificity mitogen-activated protein kinase kinase 1 (EC 2.7.12.2) | protein | 285 | 43% helix, 17% strand | Q02750 |
| E | Dual specificity mitogen-activated protein kinase kinase 1 (EC 2.7.12.2) | protein | 286 | 43% helix, 16% strand | Q02750 |
| F | SERINE/THREONINE-protein kinase B-RAF (EC 2.7.11.1) | protein | 258 | 41% helix, 17% strand | P15056 |
| G | SERINE/THREONINE-protein kinase B-RAF (EC 2.7.11.1) | protein | 259 | 41% helix, 16% strand | P15056 |
| H | Dual specificity mitogen-activated protein kinase kinase 1 (EC 2.7.12.2) | protein | 275 | 43% helix, 17% strand | Q02750 |
Ligands and binding sites
- 573 · 7-fluoro-3-[(2-fluoro-4-iodophenyl)amino]-N-{[(2S)-2-hydroxypropyl]oxy}furo[3,2-c]pyridine-2-carboxamide · ligand · 5 copies · chains A, B, D, E, F, G, H
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · 4 copies · chains A, D, E, H
- MG · Magnesium ion · metal · 4 copies · chains A, D, E, H
- CL · Chloride ion · ion · chains F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1019 | 0.86 | 0.87 | 116 | ACP, MG, 573 |
| 2 | 826 | 0.85 | 0.88 | 93 | ACP, MG, 573 |
| 3 | 893 | 0.84 | 0.86 | 94 | ACP, MG, 573 |
| 4 | 714 | 0.83 | 0.87 | 76 | ACP, MG, 573 |
| 5 | 1136 | 0.82 | 0.83 | 106 | empty |
Interfaces
10 interfaces between chains.
- A–B · 1483 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 1422 Ų buried · 11 hydrogen bonds · protein-protein
- G–H · 1375 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 1363 Ų buried · 13 hydrogen bonds · protein-protein
- F–G · 1067 Ų buried · 17 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 Q02750
- Every structure of UniProt P15056
- Elsewhere: RCSB PDB 4MNE · PDBe 4MNE · UniProt Q02750 · UniProt P15056
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