Research workbench
Structural basis for histone code recognition by BRPF2-PHD1 finger
Analyse Structural basis for histone code recognition by BRPF2-PHD1 finger in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L43
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone H3.3,LINKER,BROMODOMAIN-containing protein 1
- UniProt
- P84243, O95696
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 13% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone H3.3,LINKER,BROMODOMAIN-containing protein 1 | protein | 80 | 13% helix, 15% strand | P84243, O95696 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2L43 · Structural basis for histone code recognition by BRPF2-PHD1 finger · the same entry in another collection · chain A against A, TM-score 1.00
- O95696 · AlphaFold monomer V2.0 prediction for bromodomain-containing protein 1 (O95696) · a predicted model of the same protein · chain A against A, TM-score 0.53
- P84243 · AlphaFold monomer V2.0 prediction for histone H3.3 (P84243) · a predicted model of the same protein · chain A against A, TM-score 0.24
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 P84243
- Every structure of UniProt O95696
- Elsewhere: RCSB PDB 2L43 · PDBe 2L43 · UniProt P84243 · UniProt O95696
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