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
- 6G6K
- Type
- protein
- Length
- 329 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01106, P61244
- Ligands
- CL
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 89 | — | P01106 |
| B, D | — | protein | 76 | — | P61244 |
| C | — | protein | 88 | — | P01106 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G6K · The crystal structures of Human MYC:MAX bHLHZip complex · the same entry in another collection · chain A against A, TM-score 1.00
- P61244 · AlphaFold monomer V2.0 prediction for protein max (P61244) · a predicted model of the same protein · chain B against A, TM-score 0.96
- 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 0.92
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 6G6K · PDBe 6G6K · UniProt P01106 · UniProt P61244
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