MolNFT v1 · #49752 · protein
Structural basis of EZH2 recognition by eed
2QXV: “Structural basis of EZH2 recognition by eed”. X-ray diffraction. MolNFT v1 #49752 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2QXV
- Type
- protein
- Length
- 381 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q921E6, Q61188
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 352 | — | Q921E6 |
| B | — | protein | 29 | — | Q61188 |
Compared structures
- 2QXV · Structural basis of EZH2 recognition by EED · the same entry in another collection · chain B against B, TM-score 1.00
- Q921E6 · AlphaFold monomer V2.0 prediction for polycomb protein eed (Q921E6) · a predicted model of the same protein · chain A against A, TM-score 1.00
- Q61188 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EZH2 (Q61188) · a predicted model of the same protein · chain B against A, TM-score 0.88
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 Q921E6
- Every structure of UniProt Q61188
- Elsewhere: RCSB PDB 2QXV · PDBe 2QXV · UniProt Q921E6 · UniProt Q61188
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