ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ubiquitin carboxyl-terminal hydrolase 5

Intermolecular
Cysteine 195 and cysteine 195
Intramolecular
Cysteine 199 and cysteine 202
Cysteine 195 and cysteine 793
Cysteine 202 and cysteine 219
Cysteine 199 and cysteine 219
A redox-regulated disulphide may form between two units of Ubiquitin carboxyl-terminal hydrolase 5 at cysteines 195 and 195.

Details

Redox score ?
85
PDB code
7ms5
Structure name
structure of usp5 zinc-finger ubiquitin binding domain co-crystallized with 4-(4-(4-(3,4-difluoro-phenyl)-piperidin-1-ylsulfonyl)-phenyl)-4- oxo-butanoic acid
Structure deposition date
2021-05-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide A name
Ubiquitin carboxyl-terminal hydrolase 5
Peptide B name
Ubiquitin carboxyl-terminal hydrolase 5
Peptide A accession
P45974
Peptide B accession
P45974
Peptide A residue number
195
Peptide B residue number
195

Ligandability

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 Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5 between cysteines 199 and 202.

Details

Redox score ?
86
PDB code
3ihp
Structure name
covalent ubiquitin-usp5 complex
Structure deposition date
2009-07-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
6
% buried
6
Peptide accession
P45974-2
Residue number A
199
Residue number B
202
Peptide name
Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

Ligandability

Cysteine 199 of Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

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 Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

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 Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5 between cysteines 195 and 793.

Details

Redox score ?
83
PDB code
3ihp
Structure name
covalent ubiquitin-usp5 complex
Structure deposition date
2009-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P45974-2
Residue number A
195
Residue number B
793
Peptide name
Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

Ligandability

Cysteine 195 of Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

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 793 of Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

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 Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5 between cysteines 202 and 219.

Details

Redox score ?
81
PDB code
3ihp
Structure name
covalent ubiquitin-usp5 complex
Structure deposition date
2009-07-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
8
Peptide accession
P45974-2
Residue number A
202
Residue number B
219
Peptide name
Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

Ligandability

Cysteine 202 of Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

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 219 of Isoform Short of Ubiquitin carboxyl-terminal hydrolase 5

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 5 between cysteines 199 and 219.

Details

Redox score ?
78
PDB code
7ms5
Structure name
structure of usp5 zinc-finger ubiquitin binding domain co-crystallized with 4-(4-(4-(3,4-difluoro-phenyl)-piperidin-1-ylsulfonyl)-phenyl)-4- oxo-butanoic acid
Structure deposition date
2021-05-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
25
Peptide accession
P45974
Residue number A
199
Residue number B
219
Peptide name
Ubiquitin carboxyl-terminal hydrolase 5

Ligandability

Cysteine 199 of Ubiquitin carboxyl-terminal hydrolase 5

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 219 of Ubiquitin carboxyl-terminal hydrolase 5

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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