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a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase parkin

Intramolecular
Cysteine 122 and cysteine 157
Cysteine 194 and cysteine 197
Cysteine 209 and cysteine 249
Cysteine 321 and cysteine 333
Cysteine 152 and cysteine 157
Cysteine 209 and cysteine 245
Cysteine 194 and cysteine 219
Cysteine 125 and cysteine 157
Cysteine 122 and cysteine 125
Cysteine 293 and cysteine 316
More...
Cysteine 122 and cysteine 152
Cysteine 324 and cysteine 333
Cysteine 194 and cysteine 216
Cysteine 321 and cysteine 324
Cysteine 288 and cysteine 316
Cysteine 106 and cysteine 110
Cysteine 308 and cysteine 316
Cysteine 110 and cysteine 168
Cysteine 293 and cysteine 308
Cysteine 288 and cysteine 293
Cysteine 197 and cysteine 216
Cysteine 197 and cysteine 219
Cysteine 245 and cysteine 249
Cysteine 106 and cysteine 168
Cysteine 216 and cysteine 219
Cysteine 125 and cysteine 152
Cysteine 288 and cysteine 308
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase parkin between cysteines 122 and 157 (166 and 201 respectively in this structure).

Details

Redox score ?
88
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
13
Peptide accession
S4X0T1
Residue number A
122
Residue number B
157
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 122 of E3 ubiquitin-protein ligase parkin

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 157 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 194 and 197 (238 and 241 respectively in this structure).

Details

Redox score ?
87
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
10
Peptide accession
S4X0T1
Residue number A
194
Residue number B
197
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 194 of E3 ubiquitin-protein ligase parkin

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 197 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 209 and 249 (253 and 293 respectively in this structure).

Details

Redox score ?
87
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
6
% buried
4
Peptide accession
S4X0T1
Residue number A
209
Residue number B
249
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 209 of E3 ubiquitin-protein ligase parkin

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 249 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 321 and 333 (365 and 377 respectively in this structure).

Details

Redox score ?
87
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
6
% buried
0
Peptide accession
S4X0T1
Residue number A
321
Residue number B
333
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 321 of E3 ubiquitin-protein ligase parkin

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 333 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 152 and 157 (196 and 201 respectively in this structure).

Details

Redox score ?
86
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
16
Peptide accession
S4X0T1
Residue number A
152
Residue number B
157
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 152 of E3 ubiquitin-protein ligase parkin

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 157 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 209 and 245 (253 and 289 respectively in this structure).

Details

Redox score ?
85
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
6
% buried
20
Peptide accession
S4X0T1
Residue number A
209
Residue number B
245
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 209 of E3 ubiquitin-protein ligase parkin

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 245 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 194 and 219 (238 and 263 respectively in this structure).

Details

Redox score ?
85
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
14
Peptide accession
S4X0T1
Residue number A
194
Residue number B
219
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 194 of E3 ubiquitin-protein ligase parkin

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 219 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 125 and 157 (169 and 201 respectively in this structure).

Details

Redox score ?
84
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
7
% buried
16
Peptide accession
S4X0T1
Residue number A
125
Residue number B
157
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 125 of E3 ubiquitin-protein ligase parkin

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 157 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 122 and 125 (166 and 169 respectively in this structure).

Details

Redox score ?
84
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
6
% buried
29
Peptide accession
S4X0T1
Residue number A
122
Residue number B
125
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 122 of E3 ubiquitin-protein ligase parkin

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 125 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 293 and 316 (337 and 360 respectively in this structure).

Details

Redox score ?
84
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
11
Peptide accession
S4X0T1
Residue number A
293
Residue number B
316
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 293 of E3 ubiquitin-protein ligase parkin

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 316 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 122 and 152 (166 and 196 respectively in this structure).

Details

Redox score ?
84
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
6
% buried
28
Peptide accession
S4X0T1
Residue number A
122
Residue number B
152
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 122 of E3 ubiquitin-protein ligase parkin

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 152 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 324 and 333 (368 and 377 respectively in this structure).

Details

Redox score ?
83
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
S4X0T1
Residue number A
324
Residue number B
333
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 324 of E3 ubiquitin-protein ligase parkin

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 333 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 194 and 216 (238 and 260 respectively in this structure).

Details

Redox score ?
83
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
23
Peptide accession
S4X0T1
Residue number A
194
Residue number B
216
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 194 of E3 ubiquitin-protein ligase parkin

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 216 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 321 and 324 (365 and 368 respectively in this structure).

Details

Redox score ?
83
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
6
% buried
0
Peptide accession
S4X0T1
Residue number A
321
Residue number B
324
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 321 of E3 ubiquitin-protein ligase parkin

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 324 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 288 and 316 (332 and 360 respectively in this structure).

Details

Redox score ?
82
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
6
% buried
15
Peptide accession
S4X0T1
Residue number A
288
Residue number B
316
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 288 of E3 ubiquitin-protein ligase parkin

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 316 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 106 and 110 (150 and 154 respectively in this structure).

Details

Redox score ?
81
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
20
Peptide accession
S4X0T1
Residue number A
106
Residue number B
110
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 106 of E3 ubiquitin-protein ligase parkin

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 110 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 308 and 316 (352 and 360 respectively in this structure).

Details

Redox score ?
81
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
19
Peptide accession
S4X0T1
Residue number A
308
Residue number B
316
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 308 of E3 ubiquitin-protein ligase parkin

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 316 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 110 and 168 (154 and 212 respectively in this structure).

Details

Redox score ?
81
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
22
Peptide accession
S4X0T1
Residue number A
110
Residue number B
168
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 110 of E3 ubiquitin-protein ligase parkin

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 168 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 293 and 308 (337 and 352 respectively in this structure).

Details

Redox score ?
81
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
26
Peptide accession
S4X0T1
Residue number A
293
Residue number B
308
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 293 of E3 ubiquitin-protein ligase parkin

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 308 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 288 and 293 (332 and 337 respectively in this structure).

Details

Redox score ?
80
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
22
Peptide accession
S4X0T1
Residue number A
288
Residue number B
293
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 288 of E3 ubiquitin-protein ligase parkin

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 293 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 197 and 216 (241 and 260 respectively in this structure).

Details

Redox score ?
77
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
13
Peptide accession
S4X0T1
Residue number A
197
Residue number B
216
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 197 of E3 ubiquitin-protein ligase parkin

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 216 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 197 and 219 (241 and 263 respectively in this structure).

Details

Redox score ?
77
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
10
% buried
4
Peptide accession
S4X0T1
Residue number A
197
Residue number B
219
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 197 of E3 ubiquitin-protein ligase parkin

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 219 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 245 and 249 (289 and 293 respectively in this structure).

Details

Redox score ?
77
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
16
Peptide accession
S4X0T1
Residue number A
245
Residue number B
249
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 245 of E3 ubiquitin-protein ligase parkin

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 249 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 106 and 168 (150 and 212 respectively in this structure).

Details

Redox score ?
76
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
36
Peptide accession
S4X0T1
Residue number A
106
Residue number B
168
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 106 of E3 ubiquitin-protein ligase parkin

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 168 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 216 and 219 (260 and 263 respectively in this structure).

Details

Redox score ?
76
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
16
Peptide accession
S4X0T1
Residue number A
216
Residue number B
219
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 216 of E3 ubiquitin-protein ligase parkin

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 219 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 125 and 152 (169 and 196 respectively in this structure).

Details

Redox score ?
76
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
32
Peptide accession
S4X0T1
Residue number A
125
Residue number B
152
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 125 of E3 ubiquitin-protein ligase parkin

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 152 of E3 ubiquitin-protein ligase parkin

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 parkin between cysteines 288 and 308 (332 and 352 respectively in this structure).

Details

Redox score ?
74
PDB code
7us1
Structure name
structure of parkin (r0rb) bound to two phospho-ubiquitin molecules
Structure deposition date
2022-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
30
Peptide accession
S4X0T1
Residue number A
288
Residue number B
308
Peptide name
E3 ubiquitin-protein ligase parkin

Ligandability

Cysteine 288 of E3 ubiquitin-protein ligase parkin

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 308 of E3 ubiquitin-protein ligase parkin

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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