ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase RNF165

Intramolecular
Cysteine 294 and cysteine 320
Cysteine 331 and cysteine 334
Cysteine 294 and cysteine 297
Cysteine 297 and cysteine 320
Cysteine 312 and cysteine 334
Cysteine 312 and cysteine 331
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF165 between cysteines 294 and 320.

Details

Redox score ?
88
PDB code
5ulh
Structure name
structure of rnf165 in complex with a ubch5b~ub conjugate
Structure deposition date
2017-01-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
1
% buried
66
Peptide accession
Q6ZSG1
Residue number A
294
Residue number B
320
Peptide name
E3 ubiquitin-protein ligase RNF165

Ligandability

Cysteine 294 of E3 ubiquitin-protein ligase RNF165

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 320 of E3 ubiquitin-protein ligase RNF165

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 RNF165 between cysteines 331 and 334.

Details

Redox score ?
88
PDB code
7r70
Structure name
crystal structure of the ubark2c fusion protein
Structure deposition date
2021-06-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
3
% buried
47
Peptide accession
Q6ZSG1
Residue number A
331
Residue number B
334
Peptide name
E3 ubiquitin-protein ligase RNF165

Ligandability

Cysteine 331 of E3 ubiquitin-protein ligase RNF165

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 334 of E3 ubiquitin-protein ligase RNF165

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 RNF165 between cysteines 294 and 297.

Details

Redox score ?
75
PDB code
7r71
Structure name
crystal structure of the ubark2c-ubch5b~ub complex
Structure deposition date
2021-06-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
6
% buried
nan
Peptide accession
Q6ZSG1
Residue number A
294
Residue number B
297
Peptide name
E3 ubiquitin-protein ligase RNF165

Ligandability

Cysteine 294 of E3 ubiquitin-protein ligase RNF165

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 297 of E3 ubiquitin-protein ligase RNF165

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 RNF165 between cysteines 297 and 320. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
5ulk
Structure name
crystal structure of rnf165 in complex with a ubch5b~ub conjugate
Structure deposition date
2017-01-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
18
% buried
nan
Peptide accession
Q6ZSG1
Residue number A
297
Residue number B
320
Peptide name
E3 ubiquitin-protein ligase RNF165

Ligandability

Cysteine 297 of E3 ubiquitin-protein ligase RNF165

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 320 of E3 ubiquitin-protein ligase RNF165

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 RNF165 between cysteines 312 and 334. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5d0k
Structure name
structure of ube2d2:rnf165:ub complex
Structure deposition date
2015-08-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
18
% buried
nan
Peptide accession
Q6ZSG1
Residue number A
312
Residue number B
334
Peptide name
E3 ubiquitin-protein ligase RNF165

Ligandability

Cysteine 312 of E3 ubiquitin-protein ligase RNF165

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 334 of E3 ubiquitin-protein ligase RNF165

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 RNF165 between cysteines 312 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7r71
Structure name
crystal structure of the ubark2c-ubch5b~ub complex
Structure deposition date
2021-06-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
79
Minimum pKa ?
20
% buried
nan
Peptide accession
Q6ZSG1
Residue number A
312
Residue number B
331
Peptide name
E3 ubiquitin-protein ligase RNF165

Ligandability

Cysteine 312 of E3 ubiquitin-protein ligase RNF165

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 331 of E3 ubiquitin-protein ligase RNF165

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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