Research workbench

Apo structure of the histone chaperone ASF1A residues 1-155

Analyse Apo structure of the histone chaperone ASF1A residues 1-155 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LNY
Type: protein
Length: 1,078 residues
Chains: 7
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Histone chaperone ASF1A
UniProt: Q9Y294
Pockets: 10 · best druggability 0.81

Structure

x-ray diffraction · 4 distinct chains · 12% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, D	Histone chaperone ASF1A	protein	155	12% helix, 52% strand	Q9Y294
C, E	Histone chaperone ASF1A	protein	154	12% helix, 53% strand	Q9Y294
F	Histone chaperone ASF1A	protein	153	11% helix, 51% strand	Q9Y294
G	Histone chaperone ASF1A	protein	152	12% helix, 56% strand	Q9Y294

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	841	0.81	0.84	101	empty
2	72	0.51	0.85	25	empty
3	101	0.47	0.80	17	empty
4	122	0.42	0.76	21	empty
5	68	0.40	0.79	17	empty

Interfaces

10 interfaces between chains.

A–B · 897 Å² buried · 13 hydrogen bonds · protein-protein
A–C · 592 Å² buried · 13 hydrogen bonds · protein-protein
E–F · 510 Å² buried · 7 hydrogen bonds · protein-protein
B–E · 494 Å² buried · 6 hydrogen bonds · protein-protein
D–F · 378 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7LNY · Apo structure of the Histone chaperone ASF1A residues 1-155 · the same entry in another collection · chain G against G, TM-score 1.00
Q9Y294 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1A (Q9Y294) · a predicted model of the same protein · chain G 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 7LNY · PDBe 7LNY · UniProt Q9Y294

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