ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Cathepsin E

Intramolecular
Cysteine 109 and cysteine 114
Cysteine 314 and cysteine 351
Cysteine 272 and cysteine 276
A redox-regulated disulphide may form within Cathepsin E between cysteines 109 and 114 (56 and 61 respectively in this structure).

Details

Redox score ?
87
PDB code
1tzs
Structure name
crystal structure of an activation intermediate of cathepsin e
Structure deposition date
2004-07-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14091
Residue number A
109
Residue number B
114
Peptide name
Cathepsin E

Ligandability

Cysteine 109 of Cathepsin E

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 114 of Cathepsin E

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 E between cysteines 314 and 351 (261 and 298 respectively in this structure).

Details

Redox score ?
86
PDB code
1tzs
Structure name
crystal structure of an activation intermediate of cathepsin e
Structure deposition date
2004-07-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14091
Residue number A
314
Residue number B
351
Peptide name
Cathepsin E

Ligandability

Cysteine 314 of Cathepsin E

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 351 of Cathepsin E

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 E between cysteines 272 and 276 (219 and 223 respectively in this structure).

Details

Redox score ?
83
PDB code
1tzs
Structure name
crystal structure of an activation intermediate of cathepsin e
Structure deposition date
2004-07-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14091
Residue number A
272
Residue number B
276
Peptide name
Cathepsin E

Ligandability

Cysteine 272 of Cathepsin E

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 276 of Cathepsin E

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.

If this tool was useful for finding a disulphide, please cite: