ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Probable E3 ubiquitin-protein ligase HERC1

Intramolecular
Cysteine 2042 and cysteine 2043
Cysteine 4193 and cysteine 4246
Cysteine 4141 and cysteine 4193
Cysteine 4034 and cysteine 4088
Cysteine 2139 and cysteine 2172
Cysteine 4038 and cysteine 4088
Cysteine 4034 and cysteine 4038
Cysteine 2089 and cysteine 2172
Cysteine 4038 and cysteine 4051
Cysteine 4034 and cysteine 4051
More...
Cysteine 4088 and cysteine 4141
Cysteine 4088 and cysteine 4353
Cysteine 2139 and cysteine 2187
A redox-regulated disulphide may form within Probable E3 ubiquitin-protein ligase HERC1 between cysteines 2042 and 2043. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
4qt6
Structure name
crystal structure of the spry domain of human herc1
Structure deposition date
2014-07-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
2042
Residue number B
2043
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 2042 of Probable E3 ubiquitin-protein ligase HERC1

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 2043 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4193 and 4246. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4193
Residue number B
4246
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4193 of Probable E3 ubiquitin-protein ligase HERC1

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 4246 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4141 and 4193. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
103
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4141
Residue number B
4193
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4141 of Probable E3 ubiquitin-protein ligase HERC1

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 4193 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4034 and 4088. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4034
Residue number B
4088
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4034 of Probable E3 ubiquitin-protein ligase HERC1

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 4088 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 2139 and 2172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4qt6
Structure name
crystal structure of the spry domain of human herc1
Structure deposition date
2014-07-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
2139
Residue number B
2172
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 2139 of Probable E3 ubiquitin-protein ligase HERC1

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 2172 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4038 and 4088. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4038
Residue number B
4088
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4038 of Probable E3 ubiquitin-protein ligase HERC1

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 4088 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4034 and 4038. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
100
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4034
Residue number B
4038
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4034 of Probable E3 ubiquitin-protein ligase HERC1

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 4038 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 2089 and 2172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4qt6
Structure name
crystal structure of the spry domain of human herc1
Structure deposition date
2014-07-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
2089
Residue number B
2172
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 2089 of Probable E3 ubiquitin-protein ligase HERC1

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 2172 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4038 and 4051. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4038
Residue number B
4051
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4038 of Probable E3 ubiquitin-protein ligase HERC1

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 4051 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4034 and 4051. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4034
Residue number B
4051
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4034 of Probable E3 ubiquitin-protein ligase HERC1

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 4051 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4088 and 4141. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4088
Residue number B
4141
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4088 of Probable E3 ubiquitin-protein ligase HERC1

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 4141 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 4088 and 4353. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4o2w
Structure name
crystal structure of the third rcc1-like domain of herc1
Structure deposition date
2013-12-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
4088
Residue number B
4353
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 4088 of Probable E3 ubiquitin-protein ligase HERC1

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 4353 of Probable E3 ubiquitin-protein ligase HERC1

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 Probable E3 ubiquitin-protein ligase HERC1 between cysteines 2139 and 2187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4qt6
Structure name
crystal structure of the spry domain of human herc1
Structure deposition date
2014-07-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q15751
Residue number A
2139
Residue number B
2187
Peptide name
Probable E3 ubiquitin-protein ligase HERC1

Ligandability

Cysteine 2139 of Probable E3 ubiquitin-protein ligase HERC1

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 2187 of Probable E3 ubiquitin-protein ligase HERC1

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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