MolNFT v1 · #95395 · protein

Structure of the SPT16 middle domain reveals functional features of the histone chaperone fact

4IOY · Fact complex subunit SPT16: “Structure of the SPT16 middle domain reveals functional features of the histone chaperone fact”. X-ray diffraction, 1 ligand (PO4), 1 pocket (best druggability 0.34). MolNFT v1 #95395 on GenesisL1: 3D…

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.

Pocket	Volume (Å³)	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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