ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase SIAH1

Intramolecular
Cysteine 105 and cysteine 121
Cysteine 98 and cysteine 105
Cysteine 128 and cysteine 135
Cysteine 98 and cysteine 121
Cysteine 128 and cysteine 130
Cysteine 130 and cysteine 135
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase SIAH1 between cysteines 105 and 121.

Details

Redox score ?
88
PDB code
4i7c
Structure name
siah1 mutant bound to synthetic peptide (ace)klrpv(23p)mvrpwvr
Structure deposition date
2012-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
7
% buried
5
Peptide accession
Q8IUQ4
Residue number A
105
Residue number B
121
Peptide name
E3 ubiquitin-protein ligase SIAH1

Ligandability

Cysteine 105 of E3 ubiquitin-protein ligase SIAH1

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 121 of E3 ubiquitin-protein ligase SIAH1

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-protein ligase SIAH1 between cysteines 98 and 105.

Details

Redox score ?
87
PDB code
4x3g
Structure name
crystal structure of siah1 sina domain in complex with a usp19 peptide
Structure deposition date
2014-11-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
0
Peptide accession
Q8IUQ4
Residue number A
98
Residue number B
105
Peptide name
E3 ubiquitin-protein ligase SIAH1

Ligandability

Cysteine 98 of E3 ubiquitin-protein ligase SIAH1

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 105 of E3 ubiquitin-protein ligase SIAH1

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-protein ligase SIAH1 between cysteines 128 and 135.

Details

Redox score ?
87
PDB code
4i7c
Structure name
siah1 mutant bound to synthetic peptide (ace)klrpv(23p)mvrpwvr
Structure deposition date
2012-11-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
45
Minimum pKa ?
7
% buried
22
Peptide accession
Q8IUQ4
Residue number A
128
Residue number B
135
Peptide name
E3 ubiquitin-protein ligase SIAH1

Ligandability

Cysteine 128 of E3 ubiquitin-protein ligase SIAH1

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 135 of E3 ubiquitin-protein ligase SIAH1

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-protein ligase SIAH1 between cysteines 98 and 121.

Details

Redox score ?
81
PDB code
5wzz
Structure name
the siah e3 ubiquitin ligases promote wnt/ beta-catenin signaling through mediating wnt-induced axin degradation
Structure deposition date
2017-01-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
4
Peptide accession
Q8IUQ4
Residue number A
98
Residue number B
121
Peptide name
E3 ubiquitin-protein ligase SIAH1

Ligandability

Cysteine 98 of E3 ubiquitin-protein ligase SIAH1

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 121 of E3 ubiquitin-protein ligase SIAH1

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-protein ligase SIAH1 between cysteines 128 and 130.

Details

Redox score ?
81
PDB code
4i7d
Structure name
siah1 bound to synthetic peptide (ace)klrpvamvrp(prk)vr
Structure deposition date
2012-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
3
% buried
54
Peptide accession
Q8IUQ4
Residue number A
128
Residue number B
130
Peptide name
E3 ubiquitin-protein ligase SIAH1

Ligandability

Cysteine 128 of E3 ubiquitin-protein ligase SIAH1

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 130 of E3 ubiquitin-protein ligase SIAH1

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-protein ligase SIAH1 between cysteines 130 and 135.

Details

Redox score ?
66
PDB code
4x3g
Structure name
crystal structure of siah1 sina domain in complex with a usp19 peptide
Structure deposition date
2014-11-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
30
Peptide accession
Q8IUQ4
Residue number A
130
Residue number B
135
Peptide name
E3 ubiquitin-protein ligase SIAH1

Ligandability

Cysteine 130 of E3 ubiquitin-protein ligase SIAH1

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 135 of E3 ubiquitin-protein ligase SIAH1

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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