MolNFT v1 · #148224 · protein

Crystal structure ASF1-IP4

6F0H · Histone chaperone ASF1A: “Crystal structure ASF1-IP4”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.55). MolNFT v1 #148224 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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.

Pocket	Volume (Å³)	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 Å² buried · 17 hydrogen bonds · protein-protein
C–D · 1048 Å² buried · 17 hydrogen bonds · protein-protein
B–C · 448 Å² buried · 5 hydrogen bonds · protein-protein
A–C · 300 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 85 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6F0H · Crystal structure ASF1-ip4 · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y294 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1A (Q9Y294) · a predicted model of the same protein · chain A against A, TM-score 0.99

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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