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E3 ubiquitin-protein ligase HERC2

Intramolecular
Cysteine 2708 and cysteine 2735
Cysteine 2723 and cysteine 2726
Cysteine 2708 and cysteine 2732
Cysteine 2711 and cysteine 2735
Cysteine 2708 and cysteine 2711
Cysteine 2732 and cysteine 2735
Cysteine 2711 and cysteine 2732
Cysteine 2895 and cysteine 2902
Cysteine 721 and cysteine 768
Cysteine 458 and cysteine 768
More...
Cysteine 610 and cysteine 664
Cysteine 558 and cysteine 610
Cysteine 2808 and cysteine 2902
Cysteine 4263 and cysteine 4264
Cysteine 3106 and cysteine 3158
Cysteine 4150 and cysteine 4204
Cysteine 3158 and cysteine 3212
Cysteine 4261 and cysteine 4308
Cysteine 3269 and cysteine 3316
Cysteine 4261 and cysteine 4263
Cysteine 4150 and cysteine 4159
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase HERC2 between cysteines 2708 and 2735.

Details

Redox score ?
87
PDB code
6ww4
Structure name
crystal structure of herc2 zz domain in complex with histone h3 tail
Structure deposition date
2020-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
12
Peptide accession
O95714
Residue number A
2708
Residue number B
2735
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2708 of E3 ubiquitin-protein ligase HERC2

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 2735 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 2723 and 2726.

Details

Redox score ?
85
PDB code
6ww3
Structure name
crystal structure of herc2 zz domain in complex with sumo1 tail
Structure deposition date
2020-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
O95714
Residue number A
2723
Residue number B
2726
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2723 of E3 ubiquitin-protein ligase HERC2

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 2726 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 2708 and 2732.

Details

Redox score ?
82
PDB code
6ww3
Structure name
crystal structure of herc2 zz domain in complex with sumo1 tail
Structure deposition date
2020-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
6
% buried
23
Peptide accession
O95714
Residue number A
2708
Residue number B
2732
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2708 of E3 ubiquitin-protein ligase HERC2

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 2732 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 2711 and 2735.

Details

Redox score ?
80
PDB code
6ww4
Structure name
crystal structure of herc2 zz domain in complex with histone h3 tail
Structure deposition date
2020-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
1
Peptide accession
O95714
Residue number A
2711
Residue number B
2735
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2711 of E3 ubiquitin-protein ligase HERC2

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 2735 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 2708 and 2711.

Details

Redox score ?
78
PDB code
6ww3
Structure name
crystal structure of herc2 zz domain in complex with sumo1 tail
Structure deposition date
2020-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
7
% buried
40
Peptide accession
O95714
Residue number A
2708
Residue number B
2711
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2708 of E3 ubiquitin-protein ligase HERC2

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 2711 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 2732 and 2735.

Details

Redox score ?
76
PDB code
6ww4
Structure name
crystal structure of herc2 zz domain in complex with histone h3 tail
Structure deposition date
2020-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
9
Peptide accession
O95714
Residue number A
2732
Residue number B
2735
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2732 of E3 ubiquitin-protein ligase HERC2

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 2735 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 2711 and 2732.

Details

Redox score ?
72
PDB code
6ww3
Structure name
crystal structure of herc2 zz domain in complex with sumo1 tail
Structure deposition date
2020-05-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
8
% buried
34
Peptide accession
O95714
Residue number A
2711
Residue number B
2732
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2711 of E3 ubiquitin-protein ligase HERC2

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 2732 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 2895 and 2902.

Details

Redox score ?
62
PDB code
7rgw
Structure name
crystal structure of herc2 doc domain
Structure deposition date
2021-07-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
73
Peptide accession
O95714
Residue number A
2895
Residue number B
2902
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2895 of E3 ubiquitin-protein ligase HERC2

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 2902 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 721 and 768. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4l1m
Structure name
structure of the first rcc1-like domain of herc2
Structure deposition date
2013-06-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95714
Residue number A
721
Residue number B
768
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 721 of E3 ubiquitin-protein ligase HERC2

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 768 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 458 and 768. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4l1m
Structure name
structure of the first rcc1-like domain of herc2
Structure deposition date
2013-06-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95714
Residue number A
458
Residue number B
768
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 458 of E3 ubiquitin-protein ligase HERC2

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 768 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 610 and 664. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4l1m
Structure name
structure of the first rcc1-like domain of herc2
Structure deposition date
2013-06-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
101
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95714
Residue number A
610
Residue number B
664
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 610 of E3 ubiquitin-protein ligase HERC2

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 664 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 558 and 610. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4l1m
Structure name
structure of the first rcc1-like domain of herc2
Structure deposition date
2013-06-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
102
Minimum pKa ?
nan
% buried
nan
Peptide accession
O95714
Residue number A
558
Residue number B
610
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 558 of E3 ubiquitin-protein ligase HERC2

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 610 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 2808 and 2902. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7rgw
Structure name
crystal structure of herc2 doc domain
Structure deposition date
2021-07-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
66
Peptide accession
O95714
Residue number A
2808
Residue number B
2902
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 2808 of E3 ubiquitin-protein ligase HERC2

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 2902 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 4263 and 4264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
3kci
Structure name
the third rld domain of herc2
Structure deposition date
2009-10-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
88
Peptide accession
O95714
Residue number A
4263
Residue number B
4264
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 4263 of E3 ubiquitin-protein ligase HERC2

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 4264 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 3106 and 3158. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7q42
Structure name
crystal structure of rcc1-like domain 2 of ubiquitin ligase herc2 in complex with dxdkded motif of chromatin reader baz2b
Structure deposition date
2021-10-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
109
Minimum pKa ?
11
% buried
100
Peptide accession
O95714
Residue number A
3106
Residue number B
3158
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 3106 of E3 ubiquitin-protein ligase HERC2

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 3158 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 4150 and 4204. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3kci
Structure name
the third rld domain of herc2
Structure deposition date
2009-10-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
105
Minimum pKa ?
13
% buried
100
Peptide accession
O95714
Residue number A
4150
Residue number B
4204
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 4150 of E3 ubiquitin-protein ligase HERC2

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 4204 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 3158 and 3212. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7q46
Structure name
crystal structure of rcc1-like domain 2 of ubiquitin ligase herc2 in complex with dxdkded motif of pericentriolar material 1 protein
Structure deposition date
2021-10-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
107
Minimum pKa ?
13
% buried
100
Peptide accession
O95714
Residue number A
3158
Residue number B
3212
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 3158 of E3 ubiquitin-protein ligase HERC2

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 3212 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 4261 and 4308. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3kci
Structure name
the third rld domain of herc2
Structure deposition date
2009-10-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
105
Minimum pKa ?
13
% buried
100
Peptide accession
O95714
Residue number A
4261
Residue number B
4308
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 4261 of E3 ubiquitin-protein ligase HERC2

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 4308 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 3269 and 3316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7q41
Structure name
crystal structure of rcc1-like domain 2 of ubiquitin ligase herc2 in complex with dxdkded motif of ubiquitin-protein ligase e3a (e6ap)
Structure deposition date
2021-10-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
108
Minimum pKa ?
13
% buried
100
Peptide accession
O95714
Residue number A
3269
Residue number B
3316
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 3269 of E3 ubiquitin-protein ligase HERC2

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 3316 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 4261 and 4263. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
3kci
Structure name
the third rld domain of herc2
Structure deposition date
2009-10-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
100
Minimum pKa ?
13
% buried
100
Peptide accession
O95714
Residue number A
4261
Residue number B
4263
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 4261 of E3 ubiquitin-protein ligase HERC2

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 4263 of E3 ubiquitin-protein ligase HERC2

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 HERC2 between cysteines 4150 and 4159. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
3kci
Structure name
the third rld domain of herc2
Structure deposition date
2009-10-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
108
Minimum pKa ?
13
% buried
100
Peptide accession
O95714
Residue number A
4150
Residue number B
4159
Peptide name
E3 ubiquitin-protein ligase HERC2

Ligandability

Cysteine 4150 of E3 ubiquitin-protein ligase HERC2

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 4159 of E3 ubiquitin-protein ligase HERC2

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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