ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Intermolecular
Cysteine 1733 and cysteine 1733
Intramolecular
Cysteine 1727 and cysteine 1771 L
Cysteine 1724 and cysteine 1727 L
Cysteine 1771 and cysteine 1774
Cysteine 1727 and cysteine 1774 L
Cysteine 1724 and cysteine 1771 L
Cysteine 1724 and cysteine 1774 L
Cysteine 1908 and cysteine 1920
A redox-regulated disulphide may form between two units of Probable ubiquitin carboxyl-terminal hydrolase FAF-X at cysteines 1733 and 1733. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
5wch
Structure name
crystal structure of the catalytic domain of human usp9x
Structure deposition date
2017-06-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide A name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X
Peptide B name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X
Peptide A accession
Q93008
Peptide B accession
Q93008
Peptide A residue number
1733
Peptide B residue number
1733

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 Probable ubiquitin carboxyl-terminal hydrolase FAF-X between cysteines 1727 and 1771.

Details

Redox score ?
76
PDB code
5wch
Structure name
crystal structure of the catalytic domain of human usp9x
Structure deposition date
2017-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q93008
Residue number A
1727
Residue number B
1771
Peptide name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Ligandability

Cysteine 1727 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 1771 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 Probable ubiquitin carboxyl-terminal hydrolase FAF-X between cysteines 1724 and 1727.

Details

Redox score ?
75
PDB code
5wch
Structure name
crystal structure of the catalytic domain of human usp9x
Structure deposition date
2017-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q93008
Residue number A
1724
Residue number B
1727
Peptide name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Ligandability

Cysteine 1724 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 1727 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 Probable ubiquitin carboxyl-terminal hydrolase FAF-X between cysteines 1771 and 1774.

Details

Redox score ?
75
PDB code
5wch
Structure name
crystal structure of the catalytic domain of human usp9x
Structure deposition date
2017-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q93008
Residue number A
1771
Residue number B
1774
Peptide name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Ligandability

Cysteine 1771 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 1774 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 Probable ubiquitin carboxyl-terminal hydrolase FAF-X between cysteines 1727 and 1774.

Details

Redox score ?
74
PDB code
5wch
Structure name
crystal structure of the catalytic domain of human usp9x
Structure deposition date
2017-06-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q93008
Residue number A
1727
Residue number B
1774
Peptide name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Ligandability

Cysteine 1727 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 1774 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 Probable ubiquitin carboxyl-terminal hydrolase FAF-X between cysteines 1724 and 1771.

Details

Redox score ?
70
PDB code
5wch
Structure name
crystal structure of the catalytic domain of human usp9x
Structure deposition date
2017-06-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q93008
Residue number A
1724
Residue number B
1771
Peptide name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Ligandability

Cysteine 1724 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 1771 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 Probable ubiquitin carboxyl-terminal hydrolase FAF-X between cysteines 1724 and 1774. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
5wch
Structure name
crystal structure of the catalytic domain of human usp9x
Structure deposition date
2017-06-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q93008
Residue number A
1724
Residue number B
1774
Peptide name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Ligandability

Cysteine 1724 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 1774 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 Probable ubiquitin carboxyl-terminal hydrolase FAF-X between cysteines 1908 and 1920. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5wch
Structure name
crystal structure of the catalytic domain of human usp9x
Structure deposition date
2017-06-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q93008
Residue number A
1908
Residue number B
1920
Peptide name
Probable ubiquitin carboxyl-terminal hydrolase FAF-X

Ligandability

Cysteine 1908 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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 1920 of Probable ubiquitin carboxyl-terminal hydrolase FAF-X

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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