ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cathepsin G

Intramolecular
Cysteine 142 and cysteine 207
Cysteine 172 and cysteine 186
Cysteine 49 and cysteine 65
A redox-regulated disulphide may form within Cathepsin G between cysteines 142 and 207 (136 and 201 respectively in this structure).

Details

Redox score ?
85
PDB code
1cgh
Structure name
human cathepsin g
Structure deposition date
1996-06-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08311
Residue number A
142
Residue number B
207
Peptide name
Cathepsin G

Ligandability

Cysteine 142 of Cathepsin G

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 207 of Cathepsin G

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 Cathepsin G between cysteines 172 and 186 (167 and 181 respectively in this structure).

Details

Redox score ?
82
PDB code
6vtm
Structure name
human cathepsin-g inhibited by s
Structure deposition date
2020-02-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08311
Residue number A
172
Residue number B
186
Peptide name
Cathepsin G

Ligandability

Cysteine 172 of Cathepsin G

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 186 of Cathepsin G

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 Cathepsin G between cysteines 49 and 65 (42 and 58 respectively in this structure).

Details

Redox score ?
79
PDB code
1kyn
Structure name
cathepsin-g
Structure deposition date
2002-02-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
94
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08311
Residue number A
49
Residue number B
65
Peptide name
Cathepsin G

Ligandability

Cysteine 49 of Cathepsin G

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 65 of Cathepsin G

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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