ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Intramolecular
Cysteine 39 and cysteine 155
Cysteine 171 and cysteine 245
Cysteine 155 and cysteine 158
Cysteine 39 and cysteine 105
Cysteine 171 and cysteine 172
Cysteine 245 and cysteine 291
Cysteine 39 and cysteine 140
Cysteine 172 and cysteine 245
Cysteine 105 and cysteine 155
Cysteine 127 and cysteine 202
More...
Cysteine 105 and cysteine 140
Cysteine 62 and cysteine 245
Cysteine 171 and cysteine 291
A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 39 and 155.

Details

Redox score ?
65
PDB code
2o8g
Structure name
rat pp1c gamma complexed with mouse inhibitor-2
Structure deposition date
2006-12-12
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
100
Peptide accession
P63088
Residue number A
39
Residue number B
155
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 39 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 155 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 171 and 245.

Details

Redox score ?
63
PDB code
4ut3
Structure name
x-ray structure of the human pp1 gamma catalytic subunit treated with hydrogen peroxide
Structure deposition date
2014-07-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
95
Minimum pKa ?
9
% buried
100
Peptide accession
P36873
Residue number A
171
Residue number B
245
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

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

Cysteine 245 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 155 and 158. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
2o8g
Structure name
rat pp1c gamma complexed with mouse inhibitor-2
Structure deposition date
2006-12-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
72
Peptide accession
P63088
Residue number A
155
Residue number B
158
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 155 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 158 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 39 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4ut3
Structure name
x-ray structure of the human pp1 gamma catalytic subunit treated with hydrogen peroxide
Structure deposition date
2014-07-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
100
Peptide accession
P36873
Residue number A
39
Residue number B
105
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 39 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 105 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 171 and 172. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2o8a
Structure name
rat pp1cgamma complexed with mouse inhibitor-2
Structure deposition date
2006-12-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
P63088
Residue number A
171
Residue number B
172
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

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

Cysteine 172 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 245 and 291. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4v0v
Structure name
the crystal structure of mouse pp1g in complex with truncated human ppp1r15b (631-660)
Structure deposition date
2014-09-18
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
88
Peptide accession
P63087
Residue number A
245
Residue number B
291
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 245 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 291 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 39 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2o8a
Structure name
rat pp1cgamma complexed with mouse inhibitor-2
Structure deposition date
2006-12-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
13
% buried
95
Peptide accession
P63088
Residue number A
39
Residue number B
140
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 39 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 140 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 172 and 245. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4ut3
Structure name
x-ray structure of the human pp1 gamma catalytic subunit treated with hydrogen peroxide
Structure deposition date
2014-07-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
9
% buried
100
Peptide accession
P36873
Residue number A
172
Residue number B
245
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 172 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 245 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 105 and 155. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
1it6
Structure name
crystal structure of the complex between calyculin a and the catalytic subunit of protein phosphatase 1
Structure deposition date
2002-01-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
100
Peptide accession
P36873
Residue number A
105
Residue number B
155
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 105 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 155 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 127 and 202. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
1jk7
Structure name
crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1
Structure deposition date
2001-07-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
80
Peptide accession
P36873
Residue number A
127
Residue number B
202
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 127 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 202 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 105 and 140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4v0w
Structure name
the crystal structure of mouse pp1g in complex with truncated human ppp1r15b (631-669)
Structure deposition date
2014-09-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
99
Peptide accession
P63087
Residue number A
105
Residue number B
140
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 105 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 140 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 62 and 245. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
4ut3
Structure name
x-ray structure of the human pp1 gamma catalytic subunit treated with hydrogen peroxide
Structure deposition date
2014-07-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
99
Minimum pKa ?
9
% buried
100
Peptide accession
P36873
Residue number A
62
Residue number B
245
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

Cysteine 62 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Cysteine 245 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase PP1-gamma catalytic subunit between cysteines 171 and 291. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
1u32
Structure name
crystal structure of a protein phosphatase-1: calcineurin hybrid bound to okadaic acid
Structure deposition date
2004-07-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
18
% buried
nan
Peptide accession
P36873
Residue number A
171
Residue number B
291
Peptide name
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Ligandability

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

Cysteine 291 of Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

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