ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cathepsin L2

Intramolecular
Cysteine 135 and cysteine 178
Cysteine 270 and cysteine 323
Cysteine 169 and cysteine 211
Cysteine 135 and cysteine 138
A redox-regulated disulphide may form within Cathepsin L2 between cysteines 135 and 178 (2022 and 2065 respectively in this structure).

Details

Redox score ?
85
PDB code
1fh0
Structure name
crystal structure of human cathepsin v complexed with an irreversible vinyl sulfone inhibitor
Structure deposition date
2000-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60911
Residue number A
135
Residue number B
178
Peptide name
Cathepsin L2

Ligandability

Cysteine 135 of Cathepsin L2

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 178 of Cathepsin L2

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 L2 between cysteines 270 and 323 (379 and 432 respectively in this structure).

Details

Redox score ?
85
PDB code
7qgw
Structure name
sulfonated calpeptin is a promising drug candidate against sars-cov-2 infections
Structure deposition date
2021-12-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60911
Residue number A
270
Residue number B
323
Peptide name
Cathepsin L2

Ligandability

Cysteine 270 of Cathepsin L2

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 323 of Cathepsin L2

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 L2 between cysteines 169 and 211 (56 and 98 respectively in this structure).

Details

Redox score ?
83
PDB code
1fh0
Structure name
crystal structure of human cathepsin v complexed with an irreversible vinyl sulfone inhibitor
Structure deposition date
2000-07-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60911
Residue number A
169
Residue number B
211
Peptide name
Cathepsin L2

Ligandability

Cysteine 169 of Cathepsin L2

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 211 of Cathepsin L2

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 L2 between cysteines 135 and 138 (2022 and 2025 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
1fh0
Structure name
crystal structure of human cathepsin v complexed with an irreversible vinyl sulfone inhibitor
Structure deposition date
2000-07-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
14
% buried
nan
Peptide accession
O60911
Residue number A
135
Residue number B
138
Peptide name
Cathepsin L2

Ligandability

Cysteine 135 of Cathepsin L2

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 138 of Cathepsin L2

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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