PHD finger protein 19

Intramolecular

A redox-regulated disulphide may form within PHD finger protein 19 between cysteines 48 and 70. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6wau

Structure name

complex structure of phf19

Structure deposition date

2020-03-26

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Q5T6S3

Residue number A

Residue number B

Peptide name

PHD finger protein 19

Ligandability

Cysteine 48 of PHD finger protein 19

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.