ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase synoviolin

Intramolecular
Cysteine 307 and cysteine 329
Cysteine 326 and cysteine 329
Cysteine 291 and cysteine 294
Cysteine 291 and cysteine 315
Cysteine 307 and cysteine 326
Cysteine 294 and cysteine 315
Cysteine 291 and cysteine 326
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase synoviolin between cysteines 307 and 329 (29 and 51 respectively in this structure).

Details

Redox score ?
82
PDB code
6a3z
Structure name
zinc finger domain from the hrd1 protein
Structure deposition date
2018-06-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
3
Peptide accession
Q86TM6
Residue number A
307
Residue number B
329
Peptide name
E3 ubiquitin-protein ligase synoviolin

Ligandability

Cysteine 307 of E3 ubiquitin-protein ligase synoviolin

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 329 of E3 ubiquitin-protein ligase synoviolin

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 synoviolin between cysteines 326 and 329 (48 and 51 respectively in this structure).

Details

Redox score ?
81
PDB code
6a3z
Structure name
zinc finger domain from the hrd1 protein
Structure deposition date
2018-06-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
11
Peptide accession
Q86TM6
Residue number A
326
Residue number B
329
Peptide name
E3 ubiquitin-protein ligase synoviolin

Ligandability

Cysteine 326 of E3 ubiquitin-protein ligase synoviolin

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 329 of E3 ubiquitin-protein ligase synoviolin

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 synoviolin between cysteines 291 and 294 (13 and 16 respectively in this structure).

Details

Redox score ?
81
PDB code
6a3z
Structure name
zinc finger domain from the hrd1 protein
Structure deposition date
2018-06-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
12
Peptide accession
Q86TM6
Residue number A
291
Residue number B
294
Peptide name
E3 ubiquitin-protein ligase synoviolin

Ligandability

Cysteine 291 of E3 ubiquitin-protein ligase synoviolin

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 294 of E3 ubiquitin-protein ligase synoviolin

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 synoviolin between cysteines 291 and 315 (13 and 37 respectively in this structure).

Details

Redox score ?
80
PDB code
6a3z
Structure name
zinc finger domain from the hrd1 protein
Structure deposition date
2018-06-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
16
Peptide accession
Q86TM6
Residue number A
291
Residue number B
315
Peptide name
E3 ubiquitin-protein ligase synoviolin

Ligandability

Cysteine 291 of E3 ubiquitin-protein ligase synoviolin

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 315 of E3 ubiquitin-protein ligase synoviolin

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 synoviolin between cysteines 307 and 326 (29 and 48 respectively in this structure).

Details

Redox score ?
79
PDB code
6a3z
Structure name
zinc finger domain from the hrd1 protein
Structure deposition date
2018-06-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
10
% buried
14
Peptide accession
Q86TM6
Residue number A
307
Residue number B
326
Peptide name
E3 ubiquitin-protein ligase synoviolin

Ligandability

Cysteine 307 of E3 ubiquitin-protein ligase synoviolin

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 326 of E3 ubiquitin-protein ligase synoviolin

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 synoviolin between cysteines 294 and 315 (16 and 37 respectively in this structure).

Details

Redox score ?
75
PDB code
6a3z
Structure name
zinc finger domain from the hrd1 protein
Structure deposition date
2018-06-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
10
% buried
4
Peptide accession
Q86TM6
Residue number A
294
Residue number B
315
Peptide name
E3 ubiquitin-protein ligase synoviolin

Ligandability

Cysteine 294 of E3 ubiquitin-protein ligase synoviolin

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 315 of E3 ubiquitin-protein ligase synoviolin

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 synoviolin between cysteines 291 and 326 (13 and 48 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6a3z
Structure name
zinc finger domain from the hrd1 protein
Structure deposition date
2018-06-18
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
23
Peptide accession
Q86TM6
Residue number A
291
Residue number B
326
Peptide name
E3 ubiquitin-protein ligase synoviolin

Ligandability

Cysteine 291 of E3 ubiquitin-protein ligase synoviolin

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 326 of E3 ubiquitin-protein ligase synoviolin

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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