ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ubiquitin carboxyl-terminal hydrolase 30

Intramolecular
Cysteine 234 and cysteine 237 L
Cysteine 234 and cysteine 284 L
Cysteine 237 and cysteine 284
Cysteine 237 and cysteine 287
Cysteine 284 and cysteine 287
Cysteine 234 and cysteine 287 L
Cysteine 89 and cysteine 320 L
Cysteine 89 and cysteine 322
Cysteine 320 and cysteine 322 L
A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 30 between cysteines 234 and 237.

Details

Redox score ?
88
PDB code
5ohp
Structure name
crystal structure of usp30 (c77a) in complex with lys6-linked diubiquitin
Structure deposition date
2017-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
5
% buried
1
Peptide accession
Q70CQ3
Residue number A
234
Residue number B
237
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 234 of Ubiquitin carboxyl-terminal hydrolase 30

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 237 of Ubiquitin carboxyl-terminal hydrolase 30

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 30 between cysteines 234 and 284.

Details

Redox score ?
88
PDB code
5ohn
Structure name
crystal structure of usp30 in covalent complex with ubiquitin propargylamide (low resolution)
Structure deposition date
2017-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
0
Peptide accession
Q70CQ3
Residue number A
234
Residue number B
284
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 234 of Ubiquitin carboxyl-terminal hydrolase 30

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 284 of Ubiquitin carboxyl-terminal hydrolase 30

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 30 between cysteines 237 and 284.

Details

Redox score ?
85
PDB code
5ohk
Structure name
crystal structure of usp30 in covalent complex with ubiquitin propargylamide (high resolution)
Structure deposition date
2017-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
0
Peptide accession
Q70CQ3
Residue number A
237
Residue number B
284
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 237 of Ubiquitin carboxyl-terminal hydrolase 30

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 284 of Ubiquitin carboxyl-terminal hydrolase 30

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 30 between cysteines 237 and 287.

Details

Redox score ?
81
PDB code
5ohp
Structure name
crystal structure of usp30 (c77a) in complex with lys6-linked diubiquitin
Structure deposition date
2017-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
0
Peptide accession
Q70CQ3
Residue number A
237
Residue number B
287
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 237 of Ubiquitin carboxyl-terminal hydrolase 30

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 287 of Ubiquitin carboxyl-terminal hydrolase 30

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 30 between cysteines 284 and 287.

Details

Redox score ?
81
PDB code
5ohp
Structure name
crystal structure of usp30 (c77a) in complex with lys6-linked diubiquitin
Structure deposition date
2017-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
4
Peptide accession
Q70CQ3
Residue number A
284
Residue number B
287
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 284 of Ubiquitin carboxyl-terminal hydrolase 30

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 287 of Ubiquitin carboxyl-terminal hydrolase 30

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 30 between cysteines 234 and 287.

Details

Redox score ?
80
PDB code
8d1t
Structure name
crystal structure of human usp30 in complex with a covalent inhibitor 552 and a fab
Structure deposition date
2022-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
0
Peptide accession
Q70CQ3
Residue number A
234
Residue number B
287
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 234 of Ubiquitin carboxyl-terminal hydrolase 30

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 287 of Ubiquitin carboxyl-terminal hydrolase 30

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 30 between cysteines 89 and 320.

Details

Redox score ?
63
PDB code
8d1t
Structure name
crystal structure of human usp30 in complex with a covalent inhibitor 552 and a fab
Structure deposition date
2022-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
100
Peptide accession
Q70CQ3
Residue number A
89
Residue number B
320
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 89 of Ubiquitin carboxyl-terminal hydrolase 30

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 320 of Ubiquitin carboxyl-terminal hydrolase 30

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Ubiquitin carboxyl-terminal hydrolase 30 between cysteines 89 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5ohn
Structure name
crystal structure of usp30 in covalent complex with ubiquitin propargylamide (low resolution)
Structure deposition date
2017-07-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
100
Peptide accession
Q70CQ3
Residue number A
89
Residue number B
322
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 89 of Ubiquitin carboxyl-terminal hydrolase 30

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 322 of Ubiquitin carboxyl-terminal hydrolase 30

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 30 between cysteines 320 and 322. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
8d1t
Structure name
crystal structure of human usp30 in complex with a covalent inhibitor 552 and a fab
Structure deposition date
2022-05-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
Q70CQ3
Residue number A
320
Residue number B
322
Peptide name
Ubiquitin carboxyl-terminal hydrolase 30

Ligandability

Cysteine 320 of Ubiquitin carboxyl-terminal hydrolase 30

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 322 of Ubiquitin carboxyl-terminal hydrolase 30

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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