Research workbench
Crystal structure ASF1-IP4
Analyse Crystal structure ASF1-IP4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F0H
- Type
- protein
- Length
- 356 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone chaperone ASF1A; IP4
- UniProt
- Q9Y294
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 4 distinct chains · 17% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone chaperone ASF1A | protein | 152 | 12% helix, 54% strand | Q9Y294 |
| B | IP4 | protein | 26 | 50% helix, 15% strand | — |
| C | Histone chaperone ASF1A | protein | 153 | 12% helix, 54% strand | Q9Y294 |
| D | IP4 | protein | 25 | 52% helix, 16% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · 2 copies · chains A, C
- CIT · Citric acid · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.55 | 0.75 | 40 | empty |
| 2 | 138 | 0.49 | 0.79 | 27 | SO4 |
| 3 | 77 | 0.33 | 0.75 | 22 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1056 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1048 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 448 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 300 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 85 Ų buried · 0 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 6F0H · PDBe 6F0H · UniProt Q9Y294
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