Histone chaperone ASF1B

Intramolecular

A redox-regulated disulphide may form within Histone chaperone ASF1B 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

7vcq

Structure name

structure of viral protein bkrf4 in complex with h3

Structure deposition date

2021-09-03

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q9NVP2

Residue number A

Residue number B

Peptide name

Histone chaperone ASF1B

Ligandability

Cysteine 30 of Histone chaperone ASF1B

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.