ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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AMSH-like protease

Intramolecular
Cysteine 276 and cysteine 379
Cysteine 294 and cysteine 323
Cysteine 365 and cysteine 402
A redox-regulated disulphide may form within AMSH-like protease between cysteines 276 and 379.

Details

Redox score ?
68
PDB code
7l97
Structure name
crystal structure of stambpl1 in complex with an engineered binder
Structure deposition date
2021-01-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96FJ0
Residue number A
276
Residue number B
379
Peptide name
AMSH-like protease

Ligandability

Cysteine 276 of AMSH-like protease

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 379 of AMSH-like protease

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 AMSH-like protease between cysteines 294 and 323.

Details

Redox score ?
63
PDB code
7l97
Structure name
crystal structure of stambpl1 in complex with an engineered binder
Structure deposition date
2021-01-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96FJ0
Residue number A
294
Residue number B
323
Peptide name
AMSH-like protease

Ligandability

Cysteine 294 of AMSH-like protease

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 AMSH-like protease

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 AMSH-like protease between cysteines 365 and 402. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7l97
Structure name
crystal structure of stambpl1 in complex with an engineered binder
Structure deposition date
2021-01-02
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96FJ0
Residue number A
365
Residue number B
402
Peptide name
AMSH-like protease

Ligandability

Cysteine 365 of AMSH-like protease

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 402 of AMSH-like protease

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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