ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

E3 ubiquitin-protein ligase TRIM39

Intramolecular
Cysteine 29 and cysteine 32
Cysteine 66 and cysteine 69
Cysteine 29 and cysteine 52
Cysteine 44 and cysteine 66
Cysteine 107 and cysteine 129
Cysteine 29 and cysteine 49
Cysteine 107 and cysteine 126
Cysteine 44 and cysteine 69
Cysteine 49 and cysteine 52
Cysteine 32 and cysteine 49
More...
Cysteine 126 and cysteine 129
Cysteine 32 and cysteine 52
Cysteine 118 and cysteine 129
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 29 and 32 (18 and 21 respectively in this structure).

Details

Redox score ?
90
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
0
Peptide accession
Q9HCM9
Residue number A
29
Residue number B
32
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 29 of E3 ubiquitin-protein ligase TRIM39

Cysteine 32 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 66 and 69 (55 and 58 respectively in this structure).

Details

Redox score ?
90
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
7
% buried
0
Peptide accession
Q9HCM9
Residue number A
66
Residue number B
69
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 66 of E3 ubiquitin-protein ligase TRIM39

Cysteine 69 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 29 and 52 (18 and 41 respectively in this structure).

Details

Redox score ?
89
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
0
Peptide accession
Q9HCM9
Residue number A
29
Residue number B
52
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 29 of E3 ubiquitin-protein ligase TRIM39

Cysteine 52 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 44 and 66 (33 and 55 respectively in this structure).

Details

Redox score ?
88
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
34
Minimum pKa ?
7
% buried
0
Peptide accession
Q9HCM9
Residue number A
44
Residue number B
66
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 44 of E3 ubiquitin-protein ligase TRIM39

Cysteine 66 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 107 and 129 (11 and 33 respectively in this structure).

Details

Redox score ?
88
PDB code
2did
Structure name
one sequence two fold ? : correct fold of the zf-b-box domain from human tripartite motif protein 39
Structure deposition date
2006-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
2
Peptide accession
Q9HCM9
Residue number A
107
Residue number B
129
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 107 of E3 ubiquitin-protein ligase TRIM39

Cysteine 129 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 29 and 49 (18 and 38 respectively in this structure).

Details

Redox score ?
87
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
0
Peptide accession
Q9HCM9
Residue number A
29
Residue number B
49
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 29 of E3 ubiquitin-protein ligase TRIM39

Cysteine 49 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 107 and 126 (11 and 30 respectively in this structure).

Details

Redox score ?
87
PDB code
2dif
Structure name
one sequence two fold ? : miss fold of the zf-b-box domain from human tripartite motif protein 39
Structure deposition date
2006-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
0
Peptide accession
Q9HCM9
Residue number A
107
Residue number B
126
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 107 of E3 ubiquitin-protein ligase TRIM39

Cysteine 126 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 44 and 69 (33 and 58 respectively in this structure).

Details

Redox score ?
86
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
0
Peptide accession
Q9HCM9
Residue number A
44
Residue number B
69
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 44 of E3 ubiquitin-protein ligase TRIM39

Cysteine 69 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 49 and 52 (38 and 41 respectively in this structure).

Details

Redox score ?
83
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
0
Peptide accession
Q9HCM9
Residue number A
49
Residue number B
52
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 49 of E3 ubiquitin-protein ligase TRIM39

Cysteine 52 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 32 and 49 (21 and 38 respectively in this structure).

Details

Redox score ?
82
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
Q9HCM9
Residue number A
32
Residue number B
49
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 32 of E3 ubiquitin-protein ligase TRIM39

Cysteine 49 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 126 and 129 (30 and 33 respectively in this structure).

Details

Redox score ?
78
PDB code
2dif
Structure name
one sequence two fold ? : miss fold of the zf-b-box domain from human tripartite motif protein 39
Structure deposition date
2006-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
0
Peptide accession
Q9HCM9
Residue number A
126
Residue number B
129
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 126 of E3 ubiquitin-protein ligase TRIM39

Cysteine 129 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 32 and 52 (21 and 41 respectively in this structure).

Details

Redox score ?
77
PDB code
2ecj
Structure name
solution structure of the ring domain of the human tripartite motif- containing protein 39
Structure deposition date
2007-02-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
10
% buried
0
Peptide accession
Q9HCM9
Residue number A
32
Residue number B
52
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 32 of E3 ubiquitin-protein ligase TRIM39

Cysteine 52 of E3 ubiquitin-protein ligase TRIM39

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase TRIM39 between cysteines 118 and 129 (22 and 33 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
2did
Structure name
one sequence two fold ? : correct fold of the zf-b-box domain from human tripartite motif protein 39
Structure deposition date
2006-03-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
2
Peptide accession
Q9HCM9
Residue number A
118
Residue number B
129
Peptide name
E3 ubiquitin-protein ligase TRIM39

Ligandability

Cysteine 118 of E3 ubiquitin-protein ligase TRIM39

Cysteine 129 of E3 ubiquitin-protein ligase TRIM39

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