a tool for identifying drug-targetable redox-active disulphides

Beta-crystallin B2

Intramolecular

Cysteine 38 and cysteine 67

A redox-regulated disulphide may form within Beta-crystallin B2 between cysteines 38 and 67 (22 and 50 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

50

PDB code

Structure name

close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions

Structure deposition date

1993-12-22

Thiol separation (Å)

9

Half-sphere exposure sum ?

52

Minimum pK_a ?

9

% buried

30

Peptide accession

Residue number A

38

Residue number B

67

Peptide name

Beta-crystallin B2

Ligandability

Cysteine 38 of Beta-crystallin B2

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.

Cysteine 67 of Beta-crystallin B2

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.

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