ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dual specificity protein phosphatase CDC14B

Intramolecular
Cysteine 101 and cysteine 102
Cysteine 101 and cysteine 138
Cysteine 228 and cysteine 314
Cysteine 138 and cysteine 182
Cysteine 303 and cysteine 327
A redox-regulated disulphide may form within Dual specificity protein phosphatase CDC14B between cysteines 101 and 102. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
1ohd
Structure name
structure of cdc14 in complex with tungstate
Structure deposition date
2003-05-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60729
Residue number A
101
Residue number B
102
Peptide name
Dual specificity protein phosphatase CDC14B

Ligandability

Cysteine 101 of Dual specificity protein phosphatase CDC14B

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 102 of Dual specificity protein phosphatase CDC14B

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 Dual specificity protein phosphatase CDC14B between cysteines 101 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
1ohc
Structure name
structure of the proline directed phosphatase cdc14
Structure deposition date
2003-05-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
98
Peptide accession
O60729
Residue number A
101
Residue number B
138
Peptide name
Dual specificity protein phosphatase CDC14B

Ligandability

Cysteine 101 of Dual specificity protein phosphatase CDC14B

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 Dual specificity protein phosphatase CDC14B

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 Dual specificity protein phosphatase CDC14B between cysteines 228 and 314. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1ohc
Structure name
structure of the proline directed phosphatase cdc14
Structure deposition date
2003-05-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
9
% buried
86
Peptide accession
O60729
Residue number A
228
Residue number B
314
Peptide name
Dual specificity protein phosphatase CDC14B

Ligandability

Cysteine 228 of Dual specificity protein phosphatase CDC14B

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 Dual specificity protein phosphatase CDC14B

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 Dual specificity protein phosphatase CDC14B between cysteines 138 and 182. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1ohe
Structure name
structure of cdc14b phosphatase with a peptide ligand
Structure deposition date
2003-05-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
97
Minimum pKa ?
13
% buried
100
Peptide accession
O60729
Residue number A
138
Residue number B
182
Peptide name
Dual specificity protein phosphatase CDC14B

Ligandability

Cysteine 138 of Dual specificity protein phosphatase CDC14B

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 182 of Dual specificity protein phosphatase CDC14B

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 Dual specificity protein phosphatase CDC14B between cysteines 303 and 327. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
1ohd
Structure name
structure of cdc14 in complex with tungstate
Structure deposition date
2003-05-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
O60729
Residue number A
303
Residue number B
327
Peptide name
Dual specificity protein phosphatase CDC14B

Ligandability

Cysteine 303 of Dual specificity protein phosphatase CDC14B

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 327 of Dual specificity protein phosphatase CDC14B

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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