ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dystrophin

Intermolecular
Cysteine 433 and cysteine 433
Intramolecular
Cysteine 3120 and cysteine 3174
Cysteine 3130 and cysteine 3207
Cysteine 3229 and cysteine 3266
Cysteine 3120 and cysteine 3178
Cysteine 3174 and cysteine 3178
Cysteine 3153 and cysteine 3178
A redox-regulated disulphide may form between two units of Dystrophin at cysteines 433 and 433.

Details

Redox score ?
81
PDB code
3uun
Structure name
crystal structure of n-terminal first spectrin repeat of dystrophin
Structure deposition date
2011-11-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide A name
Dystrophin
Peptide B name
Dystrophin
Peptide A accession
P11532
Peptide B accession
P11532
Peptide A residue number
433
Peptide B residue number
433

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 Dystrophin between cysteines 3120 and 3174 (120 and 174 respectively in this structure).

Details

Redox score ?
69
PDB code
1eg3
Structure name
structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
Structure deposition date
2000-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
7
% buried
61
Peptide accession
P11532
Residue number A
3120
Residue number B
3174
Peptide name
Dystrophin

Ligandability

Cysteine 3120 of Dystrophin

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 3174 of Dystrophin

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 Dystrophin between cysteines 3130 and 3207 (130 and 207 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
1eg3
Structure name
structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
Structure deposition date
2000-02-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
62
Peptide accession
P11532
Residue number A
3130
Residue number B
3207
Peptide name
Dystrophin

Ligandability

Cysteine 3130 of Dystrophin

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 3207 of Dystrophin

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 Dystrophin between cysteines 3229 and 3266 (229 and 266 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1eg3
Structure name
structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
Structure deposition date
2000-02-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
61
Peptide accession
P11532
Residue number A
3229
Residue number B
3266
Peptide name
Dystrophin

Ligandability

Cysteine 3229 of Dystrophin

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 3266 of Dystrophin

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 Dystrophin between cysteines 3120 and 3178 (120 and 178 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1eg3
Structure name
structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
Structure deposition date
2000-02-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
75
Peptide accession
P11532
Residue number A
3120
Residue number B
3178
Peptide name
Dystrophin

Ligandability

Cysteine 3120 of Dystrophin

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 3178 of Dystrophin

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 Dystrophin between cysteines 3174 and 3178 (174 and 178 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1eg3
Structure name
structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
Structure deposition date
2000-02-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
86
Peptide accession
P11532
Residue number A
3174
Residue number B
3178
Peptide name
Dystrophin

Ligandability

Cysteine 3174 of Dystrophin

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 3178 of Dystrophin

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 Dystrophin between cysteines 3153 and 3178 (153 and 178 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
1eg3
Structure name
structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
Structure deposition date
2000-02-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
92
Peptide accession
P11532
Residue number A
3153
Residue number B
3178
Peptide name
Dystrophin

Ligandability

Cysteine 3153 of Dystrophin

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 3178 of Dystrophin

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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