Palmitoyltransferase ZDHHC17

Intramolecular

A redox-regulated disulphide may form within Palmitoyltransferase ZDHHC17 between cysteines 158 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5w7i

Structure name

x-ray structure of ankyrin repeat domain of dhhc17 in complex with snap25b peptide

Structure deposition date

2017-06-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q8IUH5

Residue number A

158

Residue number B

160

Peptide name

Palmitoyltransferase ZDHHC17

Ligandability

Cysteine 158 of Palmitoyltransferase ZDHHC17

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.