Menin

Intramolecular

A redox-regulated disulphide may form within Menin between cysteines 235 and 246 (230 and 241 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5dde

Structure name

menin in complex with mi-859

Structure deposition date

2015-08-24

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

100

Peptide accession

O00255

Residue number A

235

Residue number B

246

Peptide name

Menin

Ligandability

Cysteine 235 of Menin

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.