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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
XFact complex subunit SPT16protein24326% helix, 40% strandP32558

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11070.340.7221empty

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

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