ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin/ISG15 ligase TRIM25

Intermolecular
Cysteine 351 and cysteine 351
Cysteine 511 and cysteine 588
Intramolecular
Cysteine 16 and cysteine 33
Cysteine 16 and cysteine 36
Cysteine 13 and cysteine 16
Cysteine 13 and cysteine 33
Cysteine 13 and cysteine 36
Cysteine 33 and cysteine 36
Cysteine 28 and cysteine 50
Cysteine 28 and cysteine 53
More...
Cysteine 50 and cysteine 53
Cysteine 506 and cysteine 583
Cysteine 506 and cysteine 529
Cysteine 33 and cysteine 70
Cysteine 498 and cysteine 529
Cysteine 529 and cysteine 550
A redox-regulated disulphide may form between two units of E3 ubiquitin/ISG15 ligase TRIM25 at cysteines 351 and 351.

Details

Redox score ?
64
PDB code
5nt2
Structure name
complex of influenza a ns1 with trim25 coiled coil domain
Structure deposition date
2017-04-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
35
Peptide A name
E3 ubiquitin/ISG15 ligase TRIM25
Peptide B name
E3 ubiquitin/ISG15 ligase TRIM25
Peptide A accession
Q14258
Peptide B accession
Q14258
Peptide A residue number
351
Peptide B residue number
351

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 between two units of E3 ubiquitin/ISG15 ligase TRIM25 at cysteines 511 and 588. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4b8e
Structure name
pry-spry domain of trim25
Structure deposition date
2012-08-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
84
Peptide A name
E3 ubiquitin/ISG15 ligase TRIM25
Peptide B name
E3 ubiquitin/ISG15 ligase TRIM25
Peptide A accession
Q61510
Peptide B accession
Q61510
Peptide A residue number
511
Peptide B residue number
588

Ligandability

Cysteine 511 of E3 ubiquitin/ISG15 ligase TRIM25

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 588 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 16 and 33.

Details

Redox score ?
91
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
0
% buried
62
Peptide accession
Q14258
Residue number A
16
Residue number B
33
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 16 of E3 ubiquitin/ISG15 ligase TRIM25

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 33 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 16 and 36.

Details

Redox score ?
90
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
0
% buried
62
Peptide accession
Q14258
Residue number A
16
Residue number B
36
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 16 of E3 ubiquitin/ISG15 ligase TRIM25

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 36 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 13 and 16.

Details

Redox score ?
87
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
72
Minimum pKa ?
1
% buried
76
Peptide accession
Q14258
Residue number A
13
Residue number B
16
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 13 of E3 ubiquitin/ISG15 ligase TRIM25

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 16 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 13 and 33.

Details

Redox score ?
82
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
4
% buried
79
Peptide accession
Q14258
Residue number A
13
Residue number B
33
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 13 of E3 ubiquitin/ISG15 ligase TRIM25

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 33 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 13 and 36.

Details

Redox score ?
82
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
4
% buried
80
Peptide accession
Q14258
Residue number A
13
Residue number B
36
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 13 of E3 ubiquitin/ISG15 ligase TRIM25

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 36 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 33 and 36. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
15
% buried
64
Peptide accession
Q14258
Residue number A
33
Residue number B
36
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 33 of E3 ubiquitin/ISG15 ligase TRIM25

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 36 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 28 and 50. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
15
% buried
nan
Peptide accession
Q14258
Residue number A
28
Residue number B
50
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 28 of E3 ubiquitin/ISG15 ligase TRIM25

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 50 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 28 and 53. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
15
% buried
nan
Peptide accession
Q14258
Residue number A
28
Residue number B
53
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 28 of E3 ubiquitin/ISG15 ligase TRIM25

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 53 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 50 and 53. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
15
% buried
92
Peptide accession
Q14258
Residue number A
50
Residue number B
53
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 50 of E3 ubiquitin/ISG15 ligase TRIM25

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 53 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 506 and 583. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6fln
Structure name
crystal structure of the human trim25 coiled-coil and pryspry domains
Structure deposition date
2018-01-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
32
Peptide accession
Q14258
Residue number A
506
Residue number B
583
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 506 of E3 ubiquitin/ISG15 ligase TRIM25

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 583 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 506 and 529. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6flm
Structure name
crystal structure of the human trim25 pryspry domain
Structure deposition date
2018-01-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
66
Peptide accession
Q14258
Residue number A
506
Residue number B
529
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 506 of E3 ubiquitin/ISG15 ligase TRIM25

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 529 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 33 and 70. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5fer
Structure name
complex of trim25 ring with ubch5-ub
Structure deposition date
2015-12-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
66
Peptide accession
Q14258
Residue number A
33
Residue number B
70
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 33 of E3 ubiquitin/ISG15 ligase TRIM25

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 70 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 498 and 529. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6fln
Structure name
crystal structure of the human trim25 coiled-coil and pryspry domains
Structure deposition date
2018-01-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
82
Peptide accession
Q14258
Residue number A
498
Residue number B
529
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 498 of E3 ubiquitin/ISG15 ligase TRIM25

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 529 of E3 ubiquitin/ISG15 ligase TRIM25

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 ubiquitin/ISG15 ligase TRIM25 between cysteines 529 and 550. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6fln
Structure name
crystal structure of the human trim25 coiled-coil and pryspry domains
Structure deposition date
2018-01-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
98
Peptide accession
Q14258
Residue number A
529
Residue number B
550
Peptide name
E3 ubiquitin/ISG15 ligase TRIM25

Ligandability

Cysteine 529 of E3 ubiquitin/ISG15 ligase TRIM25

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 550 of E3 ubiquitin/ISG15 ligase TRIM25

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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