ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 SUMO-protein ligase PIAS3

Intermolecular
Cysteine 201 and cysteine 201
Intramolecular
Cysteine 343 and cysteine 366
Cysteine 343 and cysteine 369
Cysteine 391 and cysteine 394
Cysteine 366 and cysteine 369
Cysteine 195 and cysteine 197
Cysteine 338 and cysteine 343
Cysteine 391 and cysteine 406
Cysteine 327 and cysteine 338
Cysteine 338 and cysteine 366
More...
Cysteine 327 and cysteine 366
Cysteine 394 and cysteine 406
Cysteine 195 and cysteine 201
A redox-regulated disulphide may form between two units of E3 SUMO-protein ligase PIAS3 at cysteines 201 and 201.

Details

Redox score ?
74
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide A name
E3 SUMO-protein ligase PIAS3
Peptide B name
E3 SUMO-protein ligase PIAS3
Peptide A accession
Q9Y6X2
Peptide B accession
Q9Y6X2
Peptide A residue number
201
Peptide B residue number
201

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 E3 SUMO-protein ligase PIAS3 between cysteines 343 and 366.

Details

Redox score ?
78
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
343
Residue number B
366
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 343 of E3 SUMO-protein ligase PIAS3

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 366 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 343 and 369.

Details

Redox score ?
77
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
343
Residue number B
369
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 343 of E3 SUMO-protein ligase PIAS3

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 369 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 391 and 394.

Details

Redox score ?
73
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
391
Residue number B
394
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 391 of E3 SUMO-protein ligase PIAS3

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 394 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 366 and 369.

Details

Redox score ?
72
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
366
Residue number B
369
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 366 of E3 SUMO-protein ligase PIAS3

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 369 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 195 and 197. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
195
Residue number B
197
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 195 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 338 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
338
Residue number B
343
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 338 of E3 SUMO-protein ligase PIAS3

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 343 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 391 and 406. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
391
Residue number B
406
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 391 of E3 SUMO-protein ligase PIAS3

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 406 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 327 and 338. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
327
Residue number B
338
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 327 of E3 SUMO-protein ligase PIAS3

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 338 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 338 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
338
Residue number B
366
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 338 of E3 SUMO-protein ligase PIAS3

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 366 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 327 and 366. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
327
Residue number B
366
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 327 of E3 SUMO-protein ligase PIAS3

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 366 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 394 and 406. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
42
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
394
Residue number B
406
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 394 of E3 SUMO-protein ligase PIAS3

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 406 of E3 SUMO-protein ligase PIAS3

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 E3 SUMO-protein ligase PIAS3 between cysteines 195 and 201. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4mvt
Structure name
crystal structure of sumo e3 ligase pias3
Structure deposition date
2013-09-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9Y6X2
Residue number A
195
Residue number B
201
Peptide name
E3 SUMO-protein ligase PIAS3

Ligandability

Cysteine 195 of E3 SUMO-protein ligase PIAS3

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 201 of E3 SUMO-protein ligase PIAS3

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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