Symplekin

Intramolecular

A redox-regulated disulphide may form within Symplekin between cysteines 100 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

3o2t

Structure name

crystal structure of the n-terminal domain of human symplekin

Structure deposition date

2010-07-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q92797

Residue number A

100

Residue number B

157

Peptide name

Symplekin

Ligandability

Cysteine 100 of Symplekin

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.