MolNFT v1 · #85279 · protein
Symmetric dimethylation of H3 arginine 2 is a novel histone mark that supports euchromatin maintenance
4A7J: “Symmetric dimethylation of H3 arginine 2 is a novel histone mark that supports euchromatin maintenance”. X-ray diffraction. MolNFT v1 #85279 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4A7J
- Type
- protein
- Length
- 309 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P61964, Q16695
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 303 | — | P61964 |
| B | — | protein | 6 | — | Q16695 |
Compared structures
- 4A7J · Symmetric Dimethylation of H3 Arginine 2 is a Novel Histone Mark that Supports… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16695 · AlphaFold monomer V2.0 prediction for histone H3.1T (Q16695) · a predicted model of the same protein · chain B against A, TM-score 0.43
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 P61964
- Every structure of UniProt Q16695
- Elsewhere: RCSB PDB 4A7J · PDBe 4A7J · UniProt P61964 · UniProt Q16695
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