Research workbench
Structure of human ASF1A in complex with histone H3
Analyse Structure of human ASF1A in complex with histone H3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IIJ
- Type
- protein
- Length
- 174 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ASF1A protein; Histone H3
- UniProt
- Q6IA08
Structure
solution nmr · 2 distinct chains · 13% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ASF1A protein | protein | 156 | 8% helix, 54% strand | Q6IA08 |
| B | Histone H3 | protein | 18 | 61% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 829 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2IIJ · Structure of human Asf1a in complex with histone H3 · the same entry in another collection · chain B against B, 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 Q6IA08
- Elsewhere: RCSB PDB 2IIJ · PDBe 2IIJ · UniProt Q6IA08
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