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E3 ubiquitin-protein ligase BRE1A

Intramolecular
Cysteine 922 and cysteine 925
Cysteine 937 and cysteine 957
Cysteine 957 and cysteine 960
Cysteine 925 and cysteine 942
Cysteine 925 and cysteine 945
Cysteine 937 and cysteine 960
Cysteine 922 and cysteine 942
Cysteine 922 and cysteine 945
Cysteine 922 and cysteine 924
Cysteine 942 and cysteine 945
More...
Cysteine 924 and cysteine 945
Cysteine 924 and cysteine 925
Cysteine 924 and cysteine 942
Cysteine 924 and cysteine 957
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase BRE1A between cysteines 922 and 925.

Details

Redox score ?
88
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
12
Peptide accession
Q5VTR2
Residue number A
922
Residue number B
925
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 922 of E3 ubiquitin-protein ligase BRE1A

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 925 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 937 and 957.

Details

Redox score ?
87
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
10
Peptide accession
Q5VTR2
Residue number A
937
Residue number B
957
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 937 of E3 ubiquitin-protein ligase BRE1A

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 957 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 957 and 960.

Details

Redox score ?
86
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
8
Peptide accession
Q5VTR2
Residue number A
957
Residue number B
960
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 957 of E3 ubiquitin-protein ligase BRE1A

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 960 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 925 and 942.

Details

Redox score ?
84
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
10
Peptide accession
Q5VTR2
Residue number A
925
Residue number B
942
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 925 of E3 ubiquitin-protein ligase BRE1A

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 942 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 925 and 945.

Details

Redox score ?
83
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
10
Peptide accession
Q5VTR2
Residue number A
925
Residue number B
945
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 925 of E3 ubiquitin-protein ligase BRE1A

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 945 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 937 and 960.

Details

Redox score ?
82
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
33
Minimum pKa ?
8
% buried
2
Peptide accession
Q5VTR2
Residue number A
937
Residue number B
960
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 937 of E3 ubiquitin-protein ligase BRE1A

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 960 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 922 and 942.

Details

Redox score ?
81
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
22
Peptide accession
Q5VTR2
Residue number A
922
Residue number B
942
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 922 of E3 ubiquitin-protein ligase BRE1A

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 942 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 922 and 945.

Details

Redox score ?
79
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
22
Peptide accession
Q5VTR2
Residue number A
922
Residue number B
945
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 922 of E3 ubiquitin-protein ligase BRE1A

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 945 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 922 and 924.

Details

Redox score ?
76
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
7
% buried
22
Peptide accession
Q5VTR2
Residue number A
922
Residue number B
924
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 922 of E3 ubiquitin-protein ligase BRE1A

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 924 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 942 and 945.

Details

Redox score ?
74
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
20
Peptide accession
Q5VTR2
Residue number A
942
Residue number B
945
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 942 of E3 ubiquitin-protein ligase BRE1A

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 945 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 924 and 945.

Details

Redox score ?
74
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
20
Peptide accession
Q5VTR2
Residue number A
924
Residue number B
945
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 924 of E3 ubiquitin-protein ligase BRE1A

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 945 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 924 and 925.

Details

Redox score ?
71
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
10
Peptide accession
Q5VTR2
Residue number A
924
Residue number B
925
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 924 of E3 ubiquitin-protein ligase BRE1A

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 925 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 924 and 942. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
21
Peptide accession
Q5VTR2
Residue number A
924
Residue number B
942
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 924 of E3 ubiquitin-protein ligase BRE1A

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 942 of E3 ubiquitin-protein ligase BRE1A

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 BRE1A between cysteines 924 and 957. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5trb
Structure name
crystal structure of the rnf20 ring domain
Structure deposition date
2016-10-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
19
Peptide accession
Q5VTR2
Residue number A
924
Residue number B
957
Peptide name
E3 ubiquitin-protein ligase BRE1A

Ligandability

Cysteine 924 of E3 ubiquitin-protein ligase BRE1A

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 957 of E3 ubiquitin-protein ligase BRE1A

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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