ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ubiquitin carboxyl-terminal hydrolase 19

Intramolecular
Cysteine 359 and cysteine 371
Cysteine 359 and cysteine 362
Cysteine 152 and cysteine 174
Cysteine 362 and cysteine 371
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 19 between cysteines 359 and 371 (94 and 106 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
1wh0
Structure name
solution structure of the cs domain of human usp19
Structure deposition date
2004-05-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
38
Peptide accession
O94966
Residue number A
359
Residue number B
371
Peptide name
Ubiquitin carboxyl-terminal hydrolase 19

Ligandability

Cysteine 359 of Ubiquitin carboxyl-terminal hydrolase 19

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 371 of Ubiquitin carboxyl-terminal hydrolase 19

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 carboxyl-terminal hydrolase 19 between cysteines 359 and 362. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6khv
Structure name
solution structure of the cs2 domain of usp19
Structure deposition date
2019-07-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
42
Minimum pKa ?
10
% buried
16
Peptide accession
O94966
Residue number A
359
Residue number B
362
Peptide name
Ubiquitin carboxyl-terminal hydrolase 19

Ligandability

Cysteine 359 of Ubiquitin carboxyl-terminal hydrolase 19

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 362 of Ubiquitin carboxyl-terminal hydrolase 19

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 carboxyl-terminal hydrolase 19 between cysteines 152 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
6k7w
Structure name
solution structure of the cs1 domain of usp19
Structure deposition date
2019-06-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
31
Peptide accession
O94966
Residue number A
152
Residue number B
174
Peptide name
Ubiquitin carboxyl-terminal hydrolase 19

Ligandability

Cysteine 152 of Ubiquitin carboxyl-terminal hydrolase 19

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 174 of Ubiquitin carboxyl-terminal hydrolase 19

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 carboxyl-terminal hydrolase 19 between cysteines 362 and 371 (97 and 106 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1wh0
Structure name
solution structure of the cs domain of human usp19
Structure deposition date
2004-05-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
12
Peptide accession
O94966
Residue number A
362
Residue number B
371
Peptide name
Ubiquitin carboxyl-terminal hydrolase 19

Ligandability

Cysteine 362 of Ubiquitin carboxyl-terminal hydrolase 19

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 371 of Ubiquitin carboxyl-terminal hydrolase 19

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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