ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

Intramolecular
Cysteine 172 and cysteine 174
Cysteine 210 and cysteine 283
Cysteine 421 and cysteine 437
Cysteine 437 and cysteine 439
A redox-regulated disulphide may form within Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta between cysteines 172 and 174.

Details

Redox score ?
65
PDB code
4mew
Structure name
structure of the core fragment of human pr70
Structure deposition date
2013-08-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
96
Peptide accession
Q9Y5P8
Residue number A
172
Residue number B
174
Peptide name
Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

Ligandability

Cysteine 172 of Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

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 174 of Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

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 Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta between cysteines 210 and 283.

Details

Redox score ?
60
PDB code
4mew
Structure name
structure of the core fragment of human pr70
Structure deposition date
2013-08-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
49
Minimum pKa ?
10
% buried
34
Peptide accession
Q9Y5P8
Residue number A
210
Residue number B
283
Peptide name
Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

Ligandability

Cysteine 210 of Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

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 283 of Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

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 Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta between cysteines 421 and 437. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
4mew
Structure name
structure of the core fragment of human pr70
Structure deposition date
2013-08-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
40
Peptide accession
Q9Y5P8
Residue number A
421
Residue number B
437
Peptide name
Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

Ligandability

Cysteine 421 of Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

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 437 of Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

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 Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta between cysteines 437 and 439. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4mew
Structure name
structure of the core fragment of human pr70
Structure deposition date
2013-08-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
25
Peptide accession
Q9Y5P8
Residue number A
437
Residue number B
439
Peptide name
Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

Ligandability

Cysteine 437 of Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

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 439 of Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta

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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