Research workbench
NMR solution structure of the C-myc-max heterodimeric leucine zipper, NMR, minimized average structure
Analyse NMR solution structure of the C-myc-max heterodimeric leucine zipper, NMR… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A93
- Type
- protein
- Length
- 64 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01106, P28574
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 32 | — | P01106 |
| B | — | protein | 32 | — | P28574 |
Compared structures
- 1A93 · NMR solution structure of the C-myc-max heterodimeric leucine zipper, NMR, minimized… · the same entry in another collection · chain A against A, TM-score 1.00
- P01106 · AlphaFold monomer V2.0 prediction for myc proto-oncogene protein (P01106) · a predicted model of the same protein · chain A against A, TM-score 0.87
- P28574 · AlphaFold monomer V2.0 prediction for protein max (P28574) · a predicted model of the same protein · chain B against A, TM-score 0.77
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 P28574
- Elsewhere: RCSB PDB 1A93 · PDBe 1A93 · UniProt P01106 · UniProt P28574
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