Research workbench
NMR solution structure of the C-myc-max heterodimeric leucine zipper, 40 structures
Analyse NMR solution structure of the C-myc-max heterodimeric leucine zipper, 40… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2A93
- Type
- protein
- Length
- 64 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-myc-max heterodimeric leucine zipper
- UniProt
- P01106, P28574
- Ligands
- ACE, NH2
Structure
solution nmr · 2 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-myc-max heterodimeric leucine zipper | protein | 32 | 84% helix, 0% strand | P01106 |
| B | C-myc-max heterodimeric leucine zipper | protein | 32 | 81% helix, 0% strand | P28574 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B
- NH2 · Amino group · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 802 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 2A93 · NMR solution structure of the C-myc-max heterodimeric leucine zipper, 40 structures · 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 0.81
- P28574 · AlphaFold monomer V2.0 prediction for protein max (P28574) · a predicted model of the same protein · chain B against A, TM-score 0.74
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 2A93 · PDBe 2A93 · UniProt P01106 · UniProt P28574
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