Calpain-2 catalytic subunit

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of Calpain-2 catalytic subunit at cysteines 191 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

1mdw

Structure name

crystal structure of calcium-bound protease core of calpain ii reveals the basis for intrinsic inactivation

Structure deposition date

2002-08-07

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide A name

Calpain-2 catalytic subunit

Peptide B name

Calpain-2 catalytic subunit

Peptide A accession

Q07009

Peptide B accession

Q07009

Peptide A residue number

191

Peptide B residue number

191

Ligandability

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.

A redox-regulated disulphide may form within Calpain-2 catalytic subunit between cysteines 498 and 640. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?