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a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase ARIH1

Intermolecular
Cysteine 357 and cysteine 86 of Ubiquitin-conjugating enzyme E2 L3 L
Intramolecular
Cysteine 281 and cysteine 299
Cysteine 203 and cysteine 236
Cysteine 344 and cysteine 347
Cysteine 344 and cysteine 362
Cysteine 347 and cysteine 362
Cysteine 344 and cysteine 367
Cysteine 347 and cysteine 367
Cysteine 276 and cysteine 281
Cysteine 357 and cysteine 362 L
More...
Cysteine 297 and cysteine 299
Cysteine 186 and cysteine 208 L
Cysteine 362 and cysteine 367
Cysteine 186 and cysteine 189
Cysteine 231 and cysteine 236
Cysteine 276 and cysteine 297
Cysteine 304 and cysteine 307
Cysteine 307 and cysteine 317
Cysteine 203 and cysteine 231
Cysteine 327 and cysteine 418
Cysteine 276 and cysteine 299
Cysteine 375 and cysteine 389
Cysteine 372 and cysteine 375
Cysteine 281 and cysteine 297
Cysteine 304 and cysteine 317
Cysteine 468 and cysteine 532
Cysteine 344 and cysteine 357 L
Cysteine 357 and cysteine 367 L
Cysteine 372 and cysteine 389
Cysteine 189 and cysteine 211 L
Cysteine 208 and cysteine 211 L
Cysteine 189 and cysteine 208 L
Cysteine 347 and cysteine 372
Cysteine 347 and cysteine 357 L
Cysteine 344 and cysteine 372
Cysteine 367 and cysteine 372
Cysteine 362 and cysteine 372
Cysteine 186 and cysteine 211 L
Cysteine 269 and cysteine 367
Cysteine 357 and cysteine 372 L
A redox-regulated disulphide may form between cysteine 357 of E3 ubiquitin-protein ligase ARIH1 and cysteine 86 of Ubiquitin-conjugating enzyme E2 L3.

Details

Redox score ?
71
PDB code
7b5l
Structure name
ubiquitin ligation to f-box protein substrates by scf-rbr e3-e3 super- assembly: nedd8-cul1-rbx1-skp1-skp2-ckshs1-cyclin a-cdk2-p27- ube2l3~ub~arih1
Structure deposition date
2020-12-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
8
% buried
62
Peptide A name
E3 ubiquitin-protein ligase ARIH1
Peptide B name
Ubiquitin-conjugating enzyme E2 L3
Peptide A accession
Q9Y4X5
Peptide B accession
P68036
Peptide A residue number
357
Peptide B residue number
86

Ligandability

Cysteine 357 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 86 of Ubiquitin-conjugating enzyme E2 L3

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

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 ARIH1 between cysteines 281 and 299.

Details

Redox score ?
95
PDB code
4kbl
Structure name
structure of hhari, a ring-ibr-ring ubiquitin ligase: autoinhibition of an ariadne-family e3 and insights into ligation mechanism
Structure deposition date
2013-04-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
2
% buried
28
Peptide accession
Q9Y4X5
Residue number A
281
Residue number B
299
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 281 of E3 ubiquitin-protein ligase ARIH1

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 299 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 203 and 236.

Details

Redox score ?
95
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
1
% buried
60
Peptide accession
Q9Y4X5
Residue number A
203
Residue number B
236
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 203 of E3 ubiquitin-protein ligase ARIH1

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 236 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 344 and 347.

Details

Redox score ?
93
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
3
Peptide accession
Q9Y4X5
Residue number A
344
Residue number B
347
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 344 of E3 ubiquitin-protein ligase ARIH1

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 347 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 344 and 362.

Details

Redox score ?
91
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
6
% buried
3
Peptide accession
Q9Y4X5
Residue number A
344
Residue number B
362
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 344 of E3 ubiquitin-protein ligase ARIH1

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 362 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 347 and 362.

Details

Redox score ?
90
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
0
Peptide accession
Q9Y4X5
Residue number A
347
Residue number B
362
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 347 of E3 ubiquitin-protein ligase ARIH1

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 362 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 344 and 367.

Details

Redox score ?
90
PDB code
4kbl
Structure name
structure of hhari, a ring-ibr-ring ubiquitin ligase: autoinhibition of an ariadne-family e3 and insights into ligation mechanism
Structure deposition date
2013-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
2
Peptide accession
Q9Y4X5
Residue number A
344
Residue number B
367
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 344 of E3 ubiquitin-protein ligase ARIH1

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 367 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 347 and 367.

Details

Redox score ?
87
PDB code
4kc9
Structure name
structure of hhari, a ring-ibr-ring ubiquitin ligase: autoinhibition of an ariadne-family e3 and insights into ligation mechanism
Structure deposition date
2013-04-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
35
Minimum pKa ?
8
% buried
0
Peptide accession
Q9Y4X5
Residue number A
347
Residue number B
367
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 347 of E3 ubiquitin-protein ligase ARIH1

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 367 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 276 and 281.

Details

Redox score ?
86
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
7
% buried
33
Peptide accession
Q9Y4X5
Residue number A
276
Residue number B
281
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 276 of E3 ubiquitin-protein ligase ARIH1

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 281 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 357 and 362 (32 and 37 respectively in this structure).

Details

Redox score ?
85
PDB code
1wd2
Structure name
solution structure of the c-terminal ring from a ring-ibr-ring (triad) motif
Structure deposition date
2004-05-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y4X5
Residue number A
357
Residue number B
362
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 357 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 362 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 297 and 299.

Details

Redox score ?
84
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
18
Peptide accession
Q9Y4X5
Residue number A
297
Residue number B
299
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 297 of E3 ubiquitin-protein ligase ARIH1

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 299 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 186 and 208.

Details

Redox score ?
82
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
nan
Peptide accession
Q9Y4X5
Residue number A
186
Residue number B
208
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 186 of E3 ubiquitin-protein ligase ARIH1

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 208 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ARIH1 between cysteines 362 and 367.

Details

Redox score ?
82
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y4X5
Residue number A
362
Residue number B
367
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 362 of E3 ubiquitin-protein ligase ARIH1

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 367 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 186 and 189.

Details

Redox score ?
82
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
5
% buried
nan
Peptide accession
Q9Y4X5
Residue number A
186
Residue number B
189
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 186 of E3 ubiquitin-protein ligase ARIH1

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 189 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 231 and 236.

Details

Redox score ?
81
PDB code
4kbl
Structure name
structure of hhari, a ring-ibr-ring ubiquitin ligase: autoinhibition of an ariadne-family e3 and insights into ligation mechanism
Structure deposition date
2013-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
14
Peptide accession
Q9Y4X5
Residue number A
231
Residue number B
236
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 231 of E3 ubiquitin-protein ligase ARIH1

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 236 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 276 and 297.

Details

Redox score ?
81
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
67
Minimum pKa ?
8
% buried
36
Peptide accession
Q9Y4X5
Residue number A
276
Residue number B
297
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 276 of E3 ubiquitin-protein ligase ARIH1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 297 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 304 and 307.

Details

Redox score ?
79
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
57
Minimum pKa ?
7
% buried
44
Peptide accession
Q9Y4X5
Residue number A
304
Residue number B
307
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 304 of E3 ubiquitin-protein ligase ARIH1

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 307 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 307 and 317.

Details

Redox score ?
79
PDB code
4kbl
Structure name
structure of hhari, a ring-ibr-ring ubiquitin ligase: autoinhibition of an ariadne-family e3 and insights into ligation mechanism
Structure deposition date
2013-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
7
% buried
40
Peptide accession
Q9Y4X5
Residue number A
307
Residue number B
317
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 307 of E3 ubiquitin-protein ligase ARIH1

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 317 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 203 and 231.

Details

Redox score ?
79
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
26
Peptide accession
Q9Y4X5
Residue number A
203
Residue number B
231
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 203 of E3 ubiquitin-protein ligase ARIH1

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 231 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 327 and 418.

Details

Redox score ?
78
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
30
Peptide accession
Q9Y4X5
Residue number A
327
Residue number B
418
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 327 of E3 ubiquitin-protein ligase ARIH1

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 418 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 276 and 299.

Details

Redox score ?
78
PDB code
4kbl
Structure name
structure of hhari, a ring-ibr-ring ubiquitin ligase: autoinhibition of an ariadne-family e3 and insights into ligation mechanism
Structure deposition date
2013-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
27
Peptide accession
Q9Y4X5
Residue number A
276
Residue number B
299
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 276 of E3 ubiquitin-protein ligase ARIH1

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 299 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 375 and 389.

Details

Redox score ?
77
PDB code
4kbl
Structure name
structure of hhari, a ring-ibr-ring ubiquitin ligase: autoinhibition of an ariadne-family e3 and insights into ligation mechanism
Structure deposition date
2013-04-23
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
8
% buried
nan
Peptide accession
Q9Y4X5
Residue number A
375
Residue number B
389
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 375 of E3 ubiquitin-protein ligase ARIH1

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 389 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 372 and 375.

Details

Redox score ?
76
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
52
Peptide accession
Q9Y4X5
Residue number A
372
Residue number B
375
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 372 of E3 ubiquitin-protein ligase ARIH1

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 375 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 281 and 297.

Details

Redox score ?
76
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
11
% buried
34
Peptide accession
Q9Y4X5
Residue number A
281
Residue number B
297
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 281 of E3 ubiquitin-protein ligase ARIH1

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 297 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 304 and 317.

Details

Redox score ?
76
PDB code
4kbl
Structure name
structure of hhari, a ring-ibr-ring ubiquitin ligase: autoinhibition of an ariadne-family e3 and insights into ligation mechanism
Structure deposition date
2013-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
46
Peptide accession
Q9Y4X5
Residue number A
304
Residue number B
317
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 304 of E3 ubiquitin-protein ligase ARIH1

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 317 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 468 and 532.

Details

Redox score ?
73
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
8
% buried
94
Peptide accession
Q9Y4X5
Residue number A
468
Residue number B
532
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 468 of E3 ubiquitin-protein ligase ARIH1

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 532 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 344 and 357 (19 and 32 respectively in this structure).

Details

Redox score ?
71
PDB code
1wd2
Structure name
solution structure of the c-terminal ring from a ring-ibr-ring (triad) motif
Structure deposition date
2004-05-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
3
Peptide accession
Q9Y4X5
Residue number A
344
Residue number B
357
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 344 of E3 ubiquitin-protein ligase ARIH1

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 357 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ARIH1 between cysteines 357 and 367 (32 and 42 respectively in this structure).

Details

Redox score ?
71
PDB code
1wd2
Structure name
solution structure of the c-terminal ring from a ring-ibr-ring (triad) motif
Structure deposition date
2004-05-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y4X5
Residue number A
357
Residue number B
367
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 357 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 367 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 372 and 389.

Details

Redox score ?
70
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
82
Peptide accession
Q9Y4X5
Residue number A
372
Residue number B
389
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 372 of E3 ubiquitin-protein ligase ARIH1

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 389 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 189 and 211.

Details

Redox score ?
66
PDB code
5tte
Structure name
crystal structure of an rbr e3 ubiquitin ligase in complex with an e2- ub thioester intermediate mimic
Structure deposition date
2016-11-03
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
14
% buried
57
Peptide accession
Q9Y4X5
Residue number A
189
Residue number B
211
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 189 of E3 ubiquitin-protein ligase ARIH1

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 211 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ARIH1 between cysteines 208 and 211.

Details

Redox score ?
64
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
69
Minimum pKa ?
14
% buried
86
Peptide accession
Q9Y4X5
Residue number A
208
Residue number B
211
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 208 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 211 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ARIH1 between cysteines 189 and 208.

Details

Redox score ?
63
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
14
% buried
nan
Peptide accession
Q9Y4X5
Residue number A
189
Residue number B
208
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 189 of E3 ubiquitin-protein ligase ARIH1

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 208 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ARIH1 between cysteines 347 and 372 (22 and 47 respectively in this structure).

Details

Redox score ?
60
PDB code
1wd2
Structure name
solution structure of the c-terminal ring from a ring-ibr-ring (triad) motif
Structure deposition date
2004-05-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y4X5
Residue number A
347
Residue number B
372
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 347 of E3 ubiquitin-protein ligase ARIH1

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 372 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 347 and 357 (22 and 32 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
1wd2
Structure name
solution structure of the c-terminal ring from a ring-ibr-ring (triad) motif
Structure deposition date
2004-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y4X5
Residue number A
347
Residue number B
357
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 347 of E3 ubiquitin-protein ligase ARIH1

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 357 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ARIH1 between cysteines 344 and 372 (19 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
1wd2
Structure name
solution structure of the c-terminal ring from a ring-ibr-ring (triad) motif
Structure deposition date
2004-05-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
3
Peptide accession
Q9Y4X5
Residue number A
344
Residue number B
372
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 344 of E3 ubiquitin-protein ligase ARIH1

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 372 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 367 and 372 (42 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1wd2
Structure name
solution structure of the c-terminal ring from a ring-ibr-ring (triad) motif
Structure deposition date
2004-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y4X5
Residue number A
367
Residue number B
372
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 367 of E3 ubiquitin-protein ligase ARIH1

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 372 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 362 and 372 (37 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1wd2
Structure name
solution structure of the c-terminal ring from a ring-ibr-ring (triad) motif
Structure deposition date
2004-05-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
0
Peptide accession
Q9Y4X5
Residue number A
362
Residue number B
372
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 362 of E3 ubiquitin-protein ligase ARIH1

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 372 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 186 and 211. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
24
% buried
nan
Peptide accession
Q9Y4X5
Residue number A
186
Residue number B
211
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 186 of E3 ubiquitin-protein ligase ARIH1

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 211 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase ARIH1 between cysteines 269 and 367. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7b5n
Structure name
ubiquitin ligation to f-box protein substrates by scf-rbr e3-e3 super- assembly: nedd8-cul1-rbx1-ube2l3~ub~arih1
Structure deposition date
2020-12-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
50
Peptide accession
Q9Y4X5
Residue number A
269
Residue number B
367
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 269 of E3 ubiquitin-protein ligase ARIH1

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 367 of E3 ubiquitin-protein ligase ARIH1

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 ARIH1 between cysteines 357 and 372. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5udh
Structure name
hhari/arih1-ubch7~ubiquitin
Structure deposition date
2016-12-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
8
% buried
88
Peptide accession
Q9Y4X5
Residue number A
357
Residue number B
372
Peptide name
E3 ubiquitin-protein ligase ARIH1

Ligandability

Cysteine 357 of E3 ubiquitin-protein ligase ARIH1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 372 of E3 ubiquitin-protein ligase ARIH1

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.

If this tool was useful for finding a disulphide, please cite: