Research workbench
Structure of the histone H3-ASF1 chaperone interaction
Analyse Structure of the histone H3-ASF1 chaperone interaction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IDC
- Type
- protein
- Length
- 167 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-silencing protein 1 and histone H3 chimera
- UniProt
- P32447, P61830
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-silencing protein 1 and histone H3 chimera | protein | 167 | 13% helix, 46% strand | P32447, P61830 |
Compared structures
- 2IDC · Structure of the Histone H3-Asf1 Chaperone Interaction · the same entry in another collection · chain A against A, TM-score 1.00
- P32447 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (P32447) · a predicted model of the same protein · chain A against A, TM-score 0.93
- P61830 · AlphaFold monomer V2.0 prediction for histone H3 (P61830) · a predicted model of the same protein · chain A against A, TM-score 0.22
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 P32447
- Every structure of UniProt P61830
- Elsewhere: RCSB PDB 2IDC · PDBe 2IDC · UniProt P32447 · UniProt P61830
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