ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase CBL-C

Intermolecular
Cysteine 189 and cysteine 202
Intramolecular
Cysteine 145 and cysteine 168
Cysteine 164 and cysteine 168
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase CBL-C at cysteines 189 and 202.

Details

Redox score ?
72
PDB code
3vrq
Structure name
crystal structure of the tyrosine kinase binding domain of cbl-c (pl mutant)
Structure deposition date
2012-04-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
8
% buried
96
Peptide A name
E3 ubiquitin-protein ligase CBL-C
Peptide B name
E3 ubiquitin-protein ligase CBL-C
Peptide A accession
Q9ULV8
Peptide B accession
Q9ULV8
Peptide A residue number
189
Peptide B residue number
202

Ligandability

Cysteine 189 of E3 ubiquitin-protein ligase CBL-C

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 202 of E3 ubiquitin-protein ligase CBL-C

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-C between cysteines 145 and 168. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3op0
Structure name
crystal structure of cbl-c (cbl-3) tkb domain in complex with egfr py1069 peptide
Structure deposition date
2010-08-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
68
Peptide accession
Q9ULV8
Residue number A
145
Residue number B
168
Peptide name
E3 ubiquitin-protein ligase CBL-C

Ligandability

Cysteine 145 of E3 ubiquitin-protein ligase CBL-C

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 CBL-C

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-C between cysteines 164 and 168. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3vrq
Structure name
crystal structure of the tyrosine kinase binding domain of cbl-c (pl mutant)
Structure deposition date
2012-04-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
76
Peptide accession
Q9ULV8
Residue number A
164
Residue number B
168
Peptide name
E3 ubiquitin-protein ligase CBL-C

Ligandability

Cysteine 164 of E3 ubiquitin-protein ligase CBL-C

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 CBL-C

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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