Research workbench
Histone H3 recognition by nucleosome-bound PRC2 subunit EZH2.
Analyse Histone H3 recognition by nucleosome-bound PRC2 subunit EZH2. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AT8
- Type
- protein + DNA
- Length
- 1,511 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15022, P84233, P62799, Q6AZJ8, P02281
- Ligands
- ZN
Structure
electron microscopy · 12 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 312 | — | — |
| C | — | protein | 124 | — | Q15022 |
| D | — | protein | 113 | — | P84233 |
| E | — | protein | 80 | — | P62799 |
| F | — | protein | 103 | — | Q6AZJ8 |
| G | — | protein | 95 | — | P02281 |
| H | — | protein | 96 | — | P84233 |
| I | — | protein | 78 | — | P62799 |
| J | — | protein | 105 | — | Q6AZJ8 |
| K | — | protein | 93 | — | P02281 |
| T | — | dna | 156 | — | — |
| U | — | dna | 156 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7AT8 · Histone H3 recognition by nucleosome-bound PRC2 subunit EZH2. · the same entry in another collection · chain U against U, TM-score 1.00
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 Q15022
- Every structure of UniProt P84233
- Every structure of UniProt P62799
- Every structure of UniProt Q6AZJ8
- Every structure of UniProt P02281
- Elsewhere: RCSB PDB 7AT8 · PDBe 7AT8 · UniProt Q15022 · UniProt P84233 · UniProt P62799 · UniProt Q6AZJ8 · UniProt P02281
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