Research workbench

Crystal structure of snasp-ASF1A-H3.1-H4 complex

Analyse Crystal structure of snasp-ASF1A-H3.1-H4 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7V6Q
Type: protein
Length: 1,071 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone chaperone ASF1A; Histone H3.1; Histone H4; Isoform 2 of nuclear autoantigenic…
UniProt: Q9Y294, P68431, P62805, P49321
Pockets: 12 · best druggability 0.77

Structure

x-ray diffraction · 6 distinct chains · 54% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Histone chaperone ASF1A	protein	154	9% helix, 55% strand	Q9Y294
B, F	Histone H3.1	protein	96	60% helix, 3% strand	P68431
C, G	Histone H4	protein	80	59% helix, 8% strand	P62805
D	Isoform 2 of nuclear autoantigenic sperm protein	protein	212	84% helix, 0% strand	P49321
E	Histone chaperone ASF1A	protein	153	9% helix, 56% strand	Q9Y294
H	Isoform 2 of nuclear autoantigenic sperm protein	protein	200	86% helix, 0% strand	P49321

Ligands and binding sites

GOL · Glycerol · additive · 6 copies · chains A, B, C, E, F, G
1PE · Pentaethylene glycol · additive · 2 copies · chains B, C, F, G

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1179	0.77	0.79	104	empty
2	761	0.77	0.81	62	GOL
3	479	0.73	0.82	50	empty
4	421	0.73	0.83	47	empty
5	186	0.59	0.82	26	empty

Interfaces

13 interfaces between chains.

B–C · 2421 Å² buried · 20 hydrogen bonds · protein-protein
F–G · 2375 Å² buried · 19 hydrogen bonds · protein-protein
F–H · 1079 Å² buried · 19 hydrogen bonds · protein-protein
B–D · 1064 Å² buried · 22 hydrogen bonds · protein-protein
E–F · 984 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7V6Q · Crystal structure of sNASP-ASF1A-H3.1-H4 complex · the same entry in another collection · chain H against H, 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
P49321 · AlphaFold monomer V2.0 prediction for nuclear autoantigenic sperm protein (P49321) · a predicted model of the same protein · chain H 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
Every structure of UniProt P68431
Every structure of UniProt P62805
Every structure of UniProt P49321
Elsewhere: RCSB PDB 7V6Q · PDBe 7V6Q · UniProt Q9Y294 · UniProt P68431 · UniProt P62805 · UniProt P49321

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.