ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase CHIP

Intramolecular
Cysteine 83 and cysteine 103
Cysteine 48 and cysteine 69
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase CHIP between cysteines 83 and 103. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6nsv
Structure name
crystal structure of the human chip tpr domain in complex with a 5mer acetylated optimized peptide
Structure deposition date
2019-01-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
99
Peptide accession
Q9UNE7
Residue number A
83
Residue number B
103
Peptide name
E3 ubiquitin-protein ligase CHIP

Ligandability

Cysteine 83 of E3 ubiquitin-protein ligase CHIP

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 103 of E3 ubiquitin-protein ligase CHIP

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 CHIP between cysteines 48 and 69. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6nsv
Structure name
crystal structure of the human chip tpr domain in complex with a 5mer acetylated optimized peptide
Structure deposition date
2019-01-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
62
Peptide accession
Q9UNE7
Residue number A
48
Residue number B
69
Peptide name
E3 ubiquitin-protein ligase CHIP

Ligandability

Cysteine 48 of E3 ubiquitin-protein ligase CHIP

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 69 of E3 ubiquitin-protein ligase CHIP

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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