ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Intramolecular
Cysteine 170 and cysteine 244
Cysteine 38 and cysteine 154
Cysteine 154 and cysteine 157
Cysteine 170 and cysteine 171
Cysteine 38 and cysteine 104
Cysteine 170 and cysteine 290
Cysteine 244 and cysteine 290
Cysteine 38 and cysteine 139
Cysteine 126 and cysteine 201
Cysteine 104 and cysteine 139
More...
Cysteine 171 and cysteine 244
Cysteine 61 and cysteine 244
A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-beta catalytic subunit between cysteines 170 and 244 (171 and 245 respectively in this structure).

Details

Redox score ?
61
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
P62140
Residue number A
170
Residue number B
244
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 170 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 244 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 38 and 154 (39 and 155 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
100
Peptide accession
P62140
Residue number A
38
Residue number B
154
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 38 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 154 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 154 and 157 (155 and 158 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
74
Peptide accession
P62140
Residue number A
154
Residue number B
157
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 154 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 157 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 170 and 171 (171 and 172 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
P62140
Residue number A
170
Residue number B
171
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 170 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 171 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 38 and 104 (39 and 105 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
P62140
Residue number A
38
Residue number B
104
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 38 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 104 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 170 and 290 (171 and 291 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
9
% buried
90
Peptide accession
P62140
Residue number A
170
Residue number B
290
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 170 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 290 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 244 and 290 (245 and 291 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
90
Peptide accession
P62140
Residue number A
244
Residue number B
290
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 244 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 290 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 38 and 139 (39 and 140 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
13
% buried
94
Peptide accession
P62140
Residue number A
38
Residue number B
139
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 38 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 139 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 126 and 201 (127 and 202 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
92
Peptide accession
P62140
Residue number A
126
Residue number B
201
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 126 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 201 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 104 and 139 (105 and 140 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
94
Peptide accession
P62140
Residue number A
104
Residue number B
139
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 104 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 139 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 171 and 244 (172 and 245 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
12
% buried
100
Peptide accession
P62140
Residue number A
171
Residue number B
244
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 171 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 244 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 PP1-beta catalytic subunit between cysteines 61 and 244 (62 and 245 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
1s70
Structure name
complex between protein ser/thr phosphatase-1 (delta) and the myosin phosphatase targeting subunit 1 (mypt1)
Structure deposition date
2004-01-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
99
Minimum pKa ?
13
% buried
100
Peptide accession
P62140
Residue number A
61
Residue number B
244
Peptide name
Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Ligandability

Cysteine 61 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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 244 of Serine/threonine-protein phosphatase PP1-beta catalytic subunit

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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