ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ski-like protein

Intermolecular
Cysteine 401 of Mothers against decapentaplegic homolog 4 and cysteine 327
Intramolecular
Cysteine 291 and cysteine 294
Cysteine 272 and cysteine 291
Cysteine 166 and cysteine 218
Cysteine 187 and cysteine 194
Cysteine 197 and cysteine 218
Cysteine 291 and cysteine 295
Cysteine 166 and cysteine 197
Cysteine 272 and cysteine 294
Cysteine 294 and cysteine 295
More...
Cysteine 194 and cysteine 218
Cysteine 156 and cysteine 166
Cysteine 268 and cysteine 327
Cysteine 187 and cysteine 230
A redox-regulated disulphide may form between cysteine 401 of Mothers against decapentaplegic homolog 4 and cysteine 327 of Ski-like protein. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5c4v
Structure name
ski-like protein
Structure deposition date
2015-06-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
9
% buried
69
Peptide A name
Mothers against decapentaplegic homolog 4
Peptide B name
Ski-like protein
Peptide A accession
Q13485
Peptide B accession
P12757
Peptide A residue number
401
Peptide B residue number
327

Ligandability

Cysteine 401 of Mothers against decapentaplegic homolog 4

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 327 of Ski-like protein

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 Ski-like protein between cysteines 291 and 294.

Details

Redox score ?
88
PDB code
5c4v
Structure name
ski-like protein
Structure deposition date
2015-06-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
2
Peptide accession
P12757
Residue number A
291
Residue number B
294
Peptide name
Ski-like protein

Ligandability

Cysteine 291 of Ski-like protein

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 294 of Ski-like protein

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 Ski-like protein between cysteines 272 and 291.

Details

Redox score ?
84
PDB code
5c4v
Structure name
ski-like protein
Structure deposition date
2015-06-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
5
% buried
20
Peptide accession
P12757
Residue number A
272
Residue number B
291
Peptide name
Ski-like protein

Ligandability

Cysteine 272 of Ski-like protein

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 291 of Ski-like protein

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 Ski-like protein between cysteines 166 and 218.

Details

Redox score ?
78
PDB code
3eq5
Structure name
crystal structure of fragment 137 to 238 of the human ski-like protein
Structure deposition date
2008-09-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
60
Peptide accession
P12757
Residue number A
166
Residue number B
218
Peptide name
Ski-like protein

Ligandability

Cysteine 166 of Ski-like protein

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 218 of Ski-like protein

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 Ski-like protein between cysteines 187 and 194.

Details

Redox score ?
75
PDB code
3eq5
Structure name
crystal structure of fragment 137 to 238 of the human ski-like protein
Structure deposition date
2008-09-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
71
Peptide accession
P12757
Residue number A
187
Residue number B
194
Peptide name
Ski-like protein

Ligandability

Cysteine 187 of Ski-like protein

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 194 of Ski-like protein

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 Ski-like protein between cysteines 197 and 218.

Details

Redox score ?
72
PDB code
3eq5
Structure name
crystal structure of fragment 137 to 238 of the human ski-like protein
Structure deposition date
2008-09-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
51
Peptide accession
P12757
Residue number A
197
Residue number B
218
Peptide name
Ski-like protein

Ligandability

Cysteine 197 of Ski-like protein

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 218 of Ski-like protein

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 Ski-like protein between cysteines 291 and 295.

Details

Redox score ?
68
PDB code
5c4v
Structure name
ski-like protein
Structure deposition date
2015-06-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
2
Peptide accession
P12757
Residue number A
291
Residue number B
295
Peptide name
Ski-like protein

Ligandability

Cysteine 291 of Ski-like protein

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 295 of Ski-like protein

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 Ski-like protein between cysteines 166 and 197.

Details

Redox score ?
66
PDB code
3eq5
Structure name
crystal structure of fragment 137 to 238 of the human ski-like protein
Structure deposition date
2008-09-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
53
Peptide accession
P12757
Residue number A
166
Residue number B
197
Peptide name
Ski-like protein

Ligandability

Cysteine 166 of Ski-like protein

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 197 of Ski-like protein

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 Ski-like protein between cysteines 272 and 294.

Details

Redox score ?
61
PDB code
5c4v
Structure name
ski-like protein
Structure deposition date
2015-06-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
17
Peptide accession
P12757
Residue number A
272
Residue number B
294
Peptide name
Ski-like protein

Ligandability

Cysteine 272 of Ski-like protein

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 294 of Ski-like protein

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 Ski-like protein between cysteines 294 and 295. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5c4v
Structure name
ski-like protein
Structure deposition date
2015-06-18
Thiol separation (Å)
7
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
nan
Peptide accession
P12757
Residue number A
294
Residue number B
295
Peptide name
Ski-like protein

Ligandability

Cysteine 294 of Ski-like protein

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 295 of Ski-like protein

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 Ski-like protein between cysteines 194 and 218. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3eq5
Structure name
crystal structure of fragment 137 to 238 of the human ski-like protein
Structure deposition date
2008-09-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
68
Peptide accession
P12757
Residue number A
194
Residue number B
218
Peptide name
Ski-like protein

Ligandability

Cysteine 194 of Ski-like protein

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 218 of Ski-like protein

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 Ski-like protein between cysteines 156 and 166. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3eq5
Structure name
crystal structure of fragment 137 to 238 of the human ski-like protein
Structure deposition date
2008-09-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
72
Peptide accession
P12757
Residue number A
156
Residue number B
166
Peptide name
Ski-like protein

Ligandability

Cysteine 156 of Ski-like protein

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 166 of Ski-like protein

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 Ski-like protein between cysteines 268 and 327. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5c4v
Structure name
ski-like protein
Structure deposition date
2015-06-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
9
% buried
62
Peptide accession
P12757
Residue number A
268
Residue number B
327
Peptide name
Ski-like protein

Ligandability

Cysteine 268 of Ski-like protein

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 327 of Ski-like protein

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 Ski-like protein between cysteines 187 and 230. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3eq5
Structure name
crystal structure of fragment 137 to 238 of the human ski-like protein
Structure deposition date
2008-09-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
72
Peptide accession
P12757
Residue number A
187
Residue number B
230
Peptide name
Ski-like protein

Ligandability

Cysteine 187 of Ski-like protein

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 230 of Ski-like protein

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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