Research workbench
Crystal structure of max-E47
Analyse Crystal structure of max-E47 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U5V
- Type
- protein
- Length
- 62 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein max, transcription factor E2-alpha chimera
- UniProt
- P28574, P15923
- Ligands
- NO3
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein max, transcription factor E2-alpha chimera | protein | 62 | 74% helix, 0% strand | P28574, P15923 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3U5V · Crystal structure of Max-E47 · the same entry in another collection · chain A against A, TM-score 1.00
- P15923 · AlphaFold monomer V2.0 prediction for transcription factor E2-alpha (P15923) · 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 A against A, TM-score 0.73
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 P28574
- Every structure of UniProt P15923
- Elsewhere: RCSB PDB 3U5V · PDBe 3U5V · UniProt P28574 · UniProt P15923
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