ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

E3 ubiquitin-protein ligase TRIM32

Intramolecular
Cysteine 20 and cysteine 23
Cysteine 61 and cysteine 64
Cysteine 39 and cysteine 64
Cysteine 20 and cysteine 44
Cysteine 20 and cysteine 47
Cysteine 23 and cysteine 47
Cysteine 23 and cysteine 44
Cysteine 39 and cysteine 61
Cysteine 44 and cysteine 47
Cysteine 20 and cysteine 61
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 20 and 23.

Details

Redox score ?
84
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
26
Peptide accession
Q13049
Residue number A
20
Residue number B
23
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 20 of E3 ubiquitin-protein ligase TRIM32

Cysteine 23 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 61 and 64.

Details

Redox score ?
81
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
14
Peptide accession
Q13049
Residue number A
61
Residue number B
64
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 61 of E3 ubiquitin-protein ligase TRIM32

Cysteine 64 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 39 and 64.

Details

Redox score ?
81
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
17
Peptide accession
Q13049
Residue number A
39
Residue number B
64
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 39 of E3 ubiquitin-protein ligase TRIM32

Cysteine 64 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 20 and 44.

Details

Redox score ?
81
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
40
Peptide accession
Q13049
Residue number A
20
Residue number B
44
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 20 of E3 ubiquitin-protein ligase TRIM32

Cysteine 44 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 20 and 47.

Details

Redox score ?
81
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
30
Peptide accession
Q13049
Residue number A
20
Residue number B
47
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 20 of E3 ubiquitin-protein ligase TRIM32

Cysteine 47 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 23 and 47.

Details

Redox score ?
80
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
9
Peptide accession
Q13049
Residue number A
23
Residue number B
47
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 23 of E3 ubiquitin-protein ligase TRIM32

Cysteine 47 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 23 and 44.

Details

Redox score ?
77
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
20
Peptide accession
Q13049
Residue number A
23
Residue number B
44
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 23 of E3 ubiquitin-protein ligase TRIM32

Cysteine 44 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 39 and 61.

Details

Redox score ?
76
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
34
Peptide accession
Q13049
Residue number A
39
Residue number B
61
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 39 of E3 ubiquitin-protein ligase TRIM32

Cysteine 61 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 44 and 47.

Details

Redox score ?
74
PDB code
5fey
Structure name
trim32 ring
Structure deposition date
2015-12-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
22
Peptide accession
Q13049
Residue number A
44
Residue number B
47
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 44 of E3 ubiquitin-protein ligase TRIM32

Cysteine 47 of E3 ubiquitin-protein ligase TRIM32

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM32 between cysteines 20 and 61 (18 and 59 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2ct2
Structure name
solution structure of the ring domain of the tripartite motif protein 32
Structure deposition date
2005-05-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
30
Peptide accession
Q13049
Residue number A
20
Residue number B
61
Peptide name
E3 ubiquitin-protein ligase TRIM32

Ligandability

Cysteine 20 of E3 ubiquitin-protein ligase TRIM32

Cysteine 61 of E3 ubiquitin-protein ligase TRIM32

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