Alpha-crystallin A chain

Intramolecular

A redox-regulated disulphide may form within Alpha-crystallin A chain between cysteines 131 and 142. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

6t1r

Structure name

pseudo-atomic model of a 16-mer assembly of reduced recombinant human alphaa-crystallin (non domain swapped configuration)

Structure deposition date

2019-10-05

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

% buried

Peptide accession

P02489

Residue number A

131

Residue number B

142

Peptide name

Alpha-crystallin A chain

Ligandability

Cysteine 131 of Alpha-crystallin A chain

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.