ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ubiquitin thioesterase OTUB1

Intramolecular
Cysteine 91 and cysteine 212
Cysteine 21 and cysteine 107
Cysteine 21 and cysteine 111
A redox-regulated disulphide may form within Ubiquitin thioesterase OTUB1 between cysteines 91 and 212. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3von
Structure name
crystalstructure of the ubiquitin protease
Structure deposition date
2012-01-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
62
Peptide accession
Q96FW1
Residue number A
91
Residue number B
212
Peptide name
Ubiquitin thioesterase OTUB1

Ligandability

Cysteine 91 of Ubiquitin thioesterase OTUB1

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 212 of Ubiquitin thioesterase OTUB1

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 Ubiquitin thioesterase OTUB1 between cysteines 21 and 107.

Details

Redox score ?
nan
PDB code
4ddi
Structure name
crystal structure of human otub1/ubch5b~ub/ub
Structure deposition date
2012-01-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96FW1
Residue number A
21
Residue number B
107
Peptide name
Ubiquitin thioesterase OTUB1

Ligandability

Cysteine 21 of Ubiquitin thioesterase OTUB1

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 107 of Ubiquitin thioesterase OTUB1

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 21 in protein A could not be asigned to a Uniprot residue.
Cysteine 107 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Ubiquitin thioesterase OTUB1 between cysteines 21 and 111.

Details

Redox score ?
nan
PDB code
4ddg
Structure name
crystal structure of human otub1/ubch5b~ub/ub
Structure deposition date
2012-01-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
nan
Peptide accession
Q96FW1
Residue number A
21
Residue number B
111
Peptide name
Ubiquitin thioesterase OTUB1

Ligandability

Cysteine 21 of Ubiquitin thioesterase OTUB1

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 111 of Ubiquitin thioesterase OTUB1

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 21 in protein A could not be asigned to a Uniprot residue.
Cysteine 111 in protein B could not be asigned to a Uniprot residue.
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