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Crystal structure ASF1-IP3
Analyse Crystal structure ASF1-IP3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F0G
- Type
- protein
- Length
- 356 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone chaperone ASF1A; IP3
- UniProt
- Q9Y294
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Histone chaperone ASF1A | protein | 154 | 12% helix, 49% strand | Q9Y294 |
| C, D | IP3 | protein | 24 | 50% helix, 17% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.57 | 0.79 | 33 | empty |
| 2 | 235 | 0.53 | 0.77 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1054 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 1038 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 339 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 Q9Y294
- Elsewhere: RCSB PDB 6F0G · PDBe 6F0G · UniProt Q9Y294
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