ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dystrobrevin alpha

Intramolecular
Cysteine 258 and cysteine 261
Cysteine 243 and cysteine 246
Cysteine 243 and cysteine 270
Cysteine 243 and cysteine 267
Cysteine 246 and cysteine 267
Cysteine 246 and cysteine 270
Cysteine 267 and cysteine 270
A redox-regulated disulphide may form within Dystrobrevin alpha between cysteines 258 and 261 (29 and 32 respectively in this structure).

Details

Redox score ?
84
PDB code
2e5r
Structure name
solution structure of the zz domain of dystrobrevin alpha (dystrobrevin-alpha)
Structure deposition date
2006-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
1
Peptide accession
Q9Y4J8
Residue number A
258
Residue number B
261
Peptide name
Dystrobrevin alpha

Ligandability

Cysteine 258 of Dystrobrevin alpha

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 261 of Dystrobrevin alpha

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 Dystrobrevin alpha between cysteines 243 and 246 (14 and 17 respectively in this structure).

Details

Redox score ?
84
PDB code
2e5r
Structure name
solution structure of the zz domain of dystrobrevin alpha (dystrobrevin-alpha)
Structure deposition date
2006-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
16
Peptide accession
Q9Y4J8
Residue number A
243
Residue number B
246
Peptide name
Dystrobrevin alpha

Ligandability

Cysteine 243 of Dystrobrevin alpha

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 246 of Dystrobrevin alpha

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 Dystrobrevin alpha between cysteines 243 and 270 (14 and 41 respectively in this structure).

Details

Redox score ?
81
PDB code
2e5r
Structure name
solution structure of the zz domain of dystrobrevin alpha (dystrobrevin-alpha)
Structure deposition date
2006-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
24
Peptide accession
Q9Y4J8
Residue number A
243
Residue number B
270
Peptide name
Dystrobrevin alpha

Ligandability

Cysteine 243 of Dystrobrevin alpha

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 270 of Dystrobrevin alpha

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 Dystrobrevin alpha between cysteines 243 and 267 (14 and 38 respectively in this structure).

Details

Redox score ?
81
PDB code
2e5r
Structure name
solution structure of the zz domain of dystrobrevin alpha (dystrobrevin-alpha)
Structure deposition date
2006-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
23
Peptide accession
Q9Y4J8
Residue number A
243
Residue number B
267
Peptide name
Dystrobrevin alpha

Ligandability

Cysteine 243 of Dystrobrevin alpha

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 267 of Dystrobrevin alpha

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 Dystrobrevin alpha between cysteines 246 and 267 (17 and 38 respectively in this structure).

Details

Redox score ?
80
PDB code
2e5r
Structure name
solution structure of the zz domain of dystrobrevin alpha (dystrobrevin-alpha)
Structure deposition date
2006-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
9
% buried
12
Peptide accession
Q9Y4J8
Residue number A
246
Residue number B
267
Peptide name
Dystrobrevin alpha

Ligandability

Cysteine 246 of Dystrobrevin alpha

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 267 of Dystrobrevin alpha

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 Dystrobrevin alpha between cysteines 246 and 270 (17 and 41 respectively in this structure).

Details

Redox score ?
80
PDB code
2e5r
Structure name
solution structure of the zz domain of dystrobrevin alpha (dystrobrevin-alpha)
Structure deposition date
2006-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
12
Peptide accession
Q9Y4J8
Residue number A
246
Residue number B
270
Peptide name
Dystrobrevin alpha

Ligandability

Cysteine 246 of Dystrobrevin alpha

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 270 of Dystrobrevin alpha

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 Dystrobrevin alpha between cysteines 267 and 270 (38 and 41 respectively in this structure).

Details

Redox score ?
77
PDB code
2e5r
Structure name
solution structure of the zz domain of dystrobrevin alpha (dystrobrevin-alpha)
Structure deposition date
2006-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
19
Peptide accession
Q9Y4J8
Residue number A
267
Residue number B
270
Peptide name
Dystrobrevin alpha

Ligandability

Cysteine 267 of Dystrobrevin alpha

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 270 of Dystrobrevin alpha

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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