Research workbench
Structure of the SPT16 middle domain reveals functional features of the histone chaperone fact
Analyse Structure of the SPT16 middle domain reveals functional features of the histone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IOY
- Type
- protein
- Length
- 243 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fact complex subunit SPT16
- UniProt
- P32558
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Fact complex subunit SPT16 | protein | 243 | 26% helix, 40% strand | P32558 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.34 | 0.72 | 21 | empty |
Compared structures
- 4IOY · Structure of the Spt16 Middle Domain Reveals Functional Features of the Histone Chaperone… · the same entry in another collection · chain X against X, TM-score 1.00
- P32558 · AlphaFold monomer V2.0 prediction for fact complex subunit SPT16 (P32558) · a predicted model of the same protein · chain X against A, TM-score 0.96
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 P32558
- Elsewhere: RCSB PDB 4IOY · PDBe 4IOY · UniProt P32558
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