ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase CBL-B

Intramolecular
Cysteine 373 and cysteine 376
Cysteine 373 and cysteine 393
Cysteine 388 and cysteine 411
Cysteine 373 and cysteine 396
Cysteine 408 and cysteine 411
Cysteine 388 and cysteine 408
Cysteine 411 and cysteine 413
Cysteine 388 and cysteine 413
Cysteine 376 and cysteine 396
Cysteine 408 and cysteine 413
More...
Cysteine 376 and cysteine 393
Cysteine 373 and cysteine 408
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CBL-B between cysteines 373 and 376.

Details

Redox score ?
90
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
42
Minimum pKa ?
7
% buried
7
Peptide accession
Q13191
Residue number A
373
Residue number B
376
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 373 of E3 ubiquitin-protein ligase CBL-B

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 376 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 373 and 393.

Details

Redox score ?
87
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
8
Peptide accession
Q13191
Residue number A
373
Residue number B
393
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 373 of E3 ubiquitin-protein ligase CBL-B

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 393 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 388 and 411.

Details

Redox score ?
84
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
0
Peptide accession
Q13191
Residue number A
388
Residue number B
411
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 388 of E3 ubiquitin-protein ligase CBL-B

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 411 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 373 and 396.

Details

Redox score ?
82
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
7
Peptide accession
Q13191
Residue number A
373
Residue number B
396
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 373 of E3 ubiquitin-protein ligase CBL-B

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 396 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 408 and 411.

Details

Redox score ?
77
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
10
Peptide accession
Q13191
Residue number A
408
Residue number B
411
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 408 of E3 ubiquitin-protein ligase CBL-B

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 411 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 388 and 408.

Details

Redox score ?
74
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
10
Peptide accession
Q13191
Residue number A
388
Residue number B
408
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 388 of E3 ubiquitin-protein ligase CBL-B

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 408 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 411 and 413.

Details

Redox score ?
69
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
6
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
0
Peptide accession
Q13191
Residue number A
411
Residue number B
413
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 411 of E3 ubiquitin-protein ligase CBL-B

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 413 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 388 and 413. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
36
Minimum pKa ?
9
% buried
0
Peptide accession
Q13191
Residue number A
388
Residue number B
413
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 388 of E3 ubiquitin-protein ligase CBL-B

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 413 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 376 and 396. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
23
% buried
0
Peptide accession
Q13191
Residue number A
376
Residue number B
396
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 376 of E3 ubiquitin-protein ligase CBL-B

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 396 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 408 and 413. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
10
Peptide accession
Q13191
Residue number A
408
Residue number B
413
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 408 of E3 ubiquitin-protein ligase CBL-B

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 413 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 376 and 393. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
23
% buried
0
Peptide accession
Q13191
Residue number A
376
Residue number B
393
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 376 of E3 ubiquitin-protein ligase CBL-B

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 393 of E3 ubiquitin-protein ligase CBL-B

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-B between cysteines 373 and 408. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2ldr
Structure name
solution structure of helix-ring domain of cbl-b in the tyr363 phosphorylated form
Structure deposition date
2011-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
18
Peptide accession
Q13191
Residue number A
373
Residue number B
408
Peptide name
E3 ubiquitin-protein ligase CBL-B

Ligandability

Cysteine 373 of E3 ubiquitin-protein ligase CBL-B

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 408 of E3 ubiquitin-protein ligase CBL-B

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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