Cofilin-2

Intramolecular

A redox-regulated disulphide may form within Cofilin-2 between cysteines 39 and 80. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

7m0g

Structure name

magic angle spinning nmr structure of human cofilin-2 assembled on actin filaments

Structure deposition date

2021-03-10

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

Q9Y281

Residue number A

Residue number B

Peptide name

Cofilin-2

Ligandability

Cysteine 39 of Cofilin-2

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.