ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase CBL

Intramolecular
Cysteine 381 and cysteine 401
Cysteine 419 and cysteine 421
Cysteine 381 and cysteine 404
Cysteine 416 and cysteine 419
Cysteine 381 and cysteine 384
Cysteine 401 and cysteine 404
Cysteine 384 and cysteine 401
Cysteine 396 and cysteine 416
Cysteine 396 and cysteine 421
Cysteine 416 and cysteine 421
More...
Cysteine 396 and cysteine 419
Cysteine 384 and cysteine 404
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CBL between cysteines 381 and 401.

Details

Redox score ?
86
PDB code
5j3x
Structure name
structure of c-cbl y371f
Structure deposition date
2016-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
3
% buried
49
Peptide accession
P22681
Residue number A
381
Residue number B
401
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 381 of E3 ubiquitin-protein ligase CBL

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 401 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 419 and 421.

Details

Redox score ?
82
PDB code
4a49
Structure name
structure of phosphotyr371-c-cbl-ubch5b complex
Structure deposition date
2011-10-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
4
Peptide accession
P22681
Residue number A
419
Residue number B
421
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 419 of E3 ubiquitin-protein ligase CBL

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 421 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 381 and 404.

Details

Redox score ?
80
PDB code
1fbv
Structure name
structure of a cbl-ubch7 complex: ring domain function in ubiquitin- protein ligases
Structure deposition date
2000-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
5
% buried
69
Peptide accession
P22681
Residue number A
381
Residue number B
404
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 381 of E3 ubiquitin-protein ligase CBL

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 404 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 416 and 419.

Details

Redox score ?
80
PDB code
4a4b
Structure name
structure of modified phosphotyr371-c-cbl-ubch5b-zap-70 complex
Structure deposition date
2011-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
31
Peptide accession
P22681
Residue number A
416
Residue number B
419
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 416 of E3 ubiquitin-protein ligase CBL

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 419 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 381 and 384.

Details

Redox score ?
77
PDB code
5o76
Structure name
structure of phosphoy371 c-cbl in complex with zap70-peptide and ubv
Structure deposition date
2017-06-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
nan
Peptide accession
P22681
Residue number A
381
Residue number B
384
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 381 of E3 ubiquitin-protein ligase CBL

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 384 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 401 and 404.

Details

Redox score ?
76
PDB code
2k4d
Structure name
e2-c-cbl recognition is necessary but not sufficient for ubiquitination activity
Structure deposition date
2008-06-06
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
nan
Peptide accession
P22681
Residue number A
401
Residue number B
404
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 401 of E3 ubiquitin-protein ligase CBL

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 404 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 384 and 401.

Details

Redox score ?
76
PDB code
5j3x
Structure name
structure of c-cbl y371f
Structure deposition date
2016-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
8
% buried
44
Peptide accession
P22681
Residue number A
384
Residue number B
401
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 384 of E3 ubiquitin-protein ligase CBL

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 401 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 396 and 416.

Details

Redox score ?
75
PDB code
4a4c
Structure name
structure of phosphotyr371-c-cbl-ubch5b-zap-70 complex
Structure deposition date
2011-10-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
48
Peptide accession
P22681
Residue number A
396
Residue number B
416
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 396 of E3 ubiquitin-protein ligase CBL

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 416 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 396 and 421.

Details

Redox score ?
71
PDB code
5o76
Structure name
structure of phosphoy371 c-cbl in complex with zap70-peptide and ubv
Structure deposition date
2017-06-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
26
Peptide accession
P22681
Residue number A
396
Residue number B
421
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 396 of E3 ubiquitin-protein ligase CBL

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 421 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 416 and 421.

Details

Redox score ?
66
PDB code
5o76
Structure name
structure of phosphoy371 c-cbl in complex with zap70-peptide and ubv
Structure deposition date
2017-06-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
39
Peptide accession
P22681
Residue number A
416
Residue number B
421
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 416 of E3 ubiquitin-protein ligase CBL

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 421 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 396 and 419. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5j3x
Structure name
structure of c-cbl y371f
Structure deposition date
2016-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
18
% buried
nan
Peptide accession
P22681
Residue number A
396
Residue number B
419
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 396 of E3 ubiquitin-protein ligase CBL

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 419 of E3 ubiquitin-protein ligase CBL

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 CBL between cysteines 384 and 404. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
1fbv
Structure name
structure of a cbl-ubch7 complex: ring domain function in ubiquitin- protein ligases
Structure deposition date
2000-07-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
23
% buried
nan
Peptide accession
P22681
Residue number A
384
Residue number B
404
Peptide name
E3 ubiquitin-protein ligase CBL

Ligandability

Cysteine 384 of E3 ubiquitin-protein ligase CBL

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 404 of E3 ubiquitin-protein ligase CBL

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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