ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Laforin

Intermolecular
Cysteine 250 and cysteine 250
Intramolecular
Cysteine 109 and cysteine 110
Cysteine 169 and cysteine 205
A redox-regulated disulphide may form between two units of Laforin at cysteines 250 and 250.

Details

Redox score ?
61
PDB code
4r30
Structure name
structure of human laforin dual specificity phosphatase domain
Structure deposition date
2014-08-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
Laforin
Peptide B name
Laforin
Peptide A accession
O95278
Peptide B accession
O95278
Peptide A residue number
250
Peptide B residue number
250

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 Laforin between cysteines 109 and 110. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
4rkk
Structure name
structure of a product bound phosphatase
Structure deposition date
2014-10-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
40
Peptide accession
O95278
Residue number A
109
Residue number B
110
Peptide name
Laforin

Ligandability

Cysteine 109 of Laforin

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 110 of Laforin

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 Laforin between cysteines 169 and 205. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4r30
Structure name
structure of human laforin dual specificity phosphatase domain
Structure deposition date
2014-08-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
73
Peptide accession
O95278
Residue number A
169
Residue number B
205
Peptide name
Laforin

Ligandability

Cysteine 169 of Laforin

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 205 of Laforin

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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