Research workbench
Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction
Analyse Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AAD
- Type
- protein
- Length
- 569 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P21675, Q9Y294
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 264 | — | P21675 |
| B | — | protein | 153 | — | Q9Y294 |
| D | — | protein | 152 | — | Q9Y294 |
Compared structures
- 3AAD · Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y294 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1A (Q9Y294) · a predicted model of the same protein · chain D against A, TM-score 0.97
- P21675 · AlphaFold monomer V2.0 prediction for transcription initiation factor tfiid subunit 1… · a predicted model of the same protein · chain A against A, TM-score 0.49
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 P21675
- Every structure of UniProt Q9Y294
- Elsewhere: RCSB PDB 3AAD · PDBe 3AAD · UniProt P21675 · UniProt Q9Y294
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