Histone chaperone ASF1A

Intramolecular

A redox-regulated disulphide may form within Histone chaperone ASF1A between cysteines 30 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7v6q

Structure name

crystal structure of snasp-asf1a-h3

Structure deposition date

2021-08-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q9Y294

Residue number A

Residue number B

Peptide name

Histone chaperone ASF1A

Ligandability

Cysteine 30 of Histone chaperone ASF1A

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.