Research workbench
The crystal structures of human MYC:MAX bhlhzip complex
Analyse The crystal structures of human MYC:MAX bhlhzip complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G6J
- Type
- protein
- Length
- 301 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myc proto-oncogene protein; Protein max
- UniProt
- P01106, P61244
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 4 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myc proto-oncogene protein | protein | 80 | 80% helix, 0% strand | P01106 |
| B | Protein max | protein | 73 | 85% helix, 0% strand | P61244 |
| C | Myc proto-oncogene protein | protein | 78 | 79% helix, 0% strand | P01106 |
| D | Protein max | protein | 70 | 87% helix, 0% strand | P61244 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.37 | 0.74 | 24 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1705 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1644 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6G6J · The crystal structures of Human MYC:MAX bHLHZip complex · the same entry in another collection · chain D against D, TM-score 1.00
- P61244 · AlphaFold monomer V2.0 prediction for protein max (P61244) · a predicted model of the same protein · chain D against A, TM-score 0.98
- P01106 · AlphaFold monomer V2.0 prediction for myc proto-oncogene protein (P01106) · a predicted model of the same protein · chain C against A, TM-score 0.96
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 P01106
- Every structure of UniProt P61244
- Elsewhere: RCSB PDB 6G6J · PDBe 6G6J · UniProt P01106 · UniProt P61244
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