ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transmembrane protease serine 13

Intermolecular
Cysteine 317 and cysteine 434
Intramolecular
Cysteine 204 and cysteine 217
Cysteine 250 and cysteine 304
Cysteine 211 and cysteine 226
Cysteine 448 and cysteine 517
Cysteine 263 and cysteine 314
Cysteine 480 and cysteine 496
Cysteine 507 and cysteine 535
Cysteine 351 and cysteine 367
Cysteine 314 and cysteine 317
A redox-regulated disulphide may form between two units of Transmembrane protease serine 13 at cysteines 317 and 434.

Details

Redox score ?
81
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Transmembrane protease serine 13
Peptide B name
Transmembrane protease serine 13
Peptide A accession
Q9BYE2
Peptide B accession
Q9BYE2
Peptide A residue number
317
Peptide B residue number
434

Ligandability

Cysteine 317 of Transmembrane protease serine 13

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 434 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 204 and 217.

Details

Redox score ?
89
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
204
Residue number B
217
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 204 of Transmembrane protease serine 13

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 217 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 250 and 304.

Details

Redox score ?
84
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
250
Residue number B
304
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 250 of Transmembrane protease serine 13

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 304 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 211 and 226.

Details

Redox score ?
82
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
74
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
211
Residue number B
226
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 211 of Transmembrane protease serine 13

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 226 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 448 and 517.

Details

Redox score ?
82
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
448
Residue number B
517
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 448 of Transmembrane protease serine 13

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 517 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 263 and 314.

Details

Redox score ?
81
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
263
Residue number B
314
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 263 of Transmembrane protease serine 13

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 314 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 480 and 496.

Details

Redox score ?
80
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
480
Residue number B
496
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 480 of Transmembrane protease serine 13

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 496 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 507 and 535.

Details

Redox score ?
79
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
507
Residue number B
535
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 507 of Transmembrane protease serine 13

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 535 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 351 and 367.

Details

Redox score ?
79
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
89
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
351
Residue number B
367
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 351 of Transmembrane protease serine 13

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 367 of Transmembrane protease serine 13

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 Transmembrane protease serine 13 between cysteines 314 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6kd5
Structure name
crystal structure of the extracellular domain of mspl/tmprss13 in complex with dec-rvkr-cmk inhibitor
Structure deposition date
2019-06-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9BYE2
Residue number A
314
Residue number B
317
Peptide name
Transmembrane protease serine 13

Ligandability

Cysteine 314 of Transmembrane protease serine 13

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 317 of Transmembrane protease serine 13

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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