Myotilin

Intramolecular

A redox-regulated disulphide may form within Myotilin between cysteines 370 and 434 (37 and 101 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

2kkq

Structure name

solution nmr structure of the ig-like c2-type 2 domain of human myotilin

Structure deposition date

2009-06-29

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q9UBF9

Residue number A

370

Residue number B

434

Peptide name

Myotilin

Ligandability

Cysteine 370 of Myotilin

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.