ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Intermolecular
Cysteine 273 and cysteine 61 of E3 ubiquitin-protein ligase PPP1R11
Cysteine 273 and cysteine 60 of E3 ubiquitin-protein ligase PPP1R11
Cysteine 273 and cysteine 273
Intramolecular
Cysteine 39 and cysteine 155
Cysteine 171 and cysteine 245
Cysteine 155 and cysteine 158
Cysteine 39 and cysteine 105
Cysteine 245 and cysteine 291
Cysteine 171 and cysteine 291
Cysteine 39 and cysteine 140
More...
Cysteine 171 and cysteine 172
Cysteine 127 and cysteine 202
Cysteine 105 and cysteine 140
Cysteine 105 and cysteine 155
Cysteine 172 and cysteine 245
Cysteine 62 and cysteine 245
A redox-regulated disulphide may form between cysteine 273 of Serine/threonine-protein phosphatase PP1-alpha catalytic subunit and cysteine 61 of E3 ubiquitin-protein ligase PPP1R11.

Details

Redox score ?
78
PDB code
8dwl
Structure name
inhibitor-3:pp1 coexpressed complex
Structure deposition date
2022-08-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
9
% buried
40
Peptide A name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Peptide B name
E3 ubiquitin-protein ligase PPP1R11
Peptide A accession
P62136
Peptide B accession
O60927
Peptide A residue number
273
Peptide B residue number
61

Ligandability

Cysteine 273 of Serine/threonine-protein phosphatase PP1-alpha 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 61 of E3 ubiquitin-protein ligase PPP1R11

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 between cysteine 273 of Serine/threonine-protein phosphatase PP1-alpha catalytic subunit and cysteine 60 of E3 ubiquitin-protein ligase PPP1R11. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
8dwl
Structure name
inhibitor-3:pp1 coexpressed complex
Structure deposition date
2022-08-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
60
Peptide A name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Peptide B name
E3 ubiquitin-protein ligase PPP1R11
Peptide A accession
P62136
Peptide B accession
O60927
Peptide A residue number
273
Peptide B residue number
60

Ligandability

Cysteine 273 of Serine/threonine-protein phosphatase PP1-alpha 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 60 of E3 ubiquitin-protein ligase PPP1R11

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 between two units of Serine/threonine-protein phosphatase PP1-alpha catalytic subunit at cysteines 273 and 273. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7t0y
Structure name
the ribosomal rna processing 1b protein phosphatase-1 holoenzyme
Structure deposition date
2021-11-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
79
Peptide A name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Peptide B name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Peptide A accession
P62136
Peptide B accession
P62136
Peptide A residue number
273
Peptide B residue number
273

Ligandability

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-alpha catalytic subunit between cysteines 39 and 155.

Details

Redox score ?
64
PDB code
6obu
Structure name
pp1 y134k in complex with microcystin lr
Structure deposition date
2019-03-21
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
100
Peptide accession
P62136
Residue number A
39
Residue number B
155
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 39 of Serine/threonine-protein phosphatase PP1-alpha 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 155 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha catalytic subunit between cysteines 171 and 245.

Details

Redox score ?
63
PDB code
6obr
Structure name
pp1 y134a in complex with microcystin lr
Structure deposition date
2019-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
100
Peptide accession
P62136
Residue number A
171
Residue number B
245
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 171 of Serine/threonine-protein phosphatase PP1-alpha 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 245 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
53
PDB code
8dwk
Structure name
inhibitor-3:pp1 reconstituted complex
Structure deposition date
2022-08-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
72
Peptide accession
P62136
Residue number A
155
Residue number B
158
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 155 of Serine/threonine-protein phosphatase PP1-alpha 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 158 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
52
PDB code
7nzm
Structure name
cryo-em structure of pre-dephosphorylation complex of phosphorylated eif2alpha with trapped holophosphatase (pp1a_d64a/ppp1r15a/g- actin/dnase i)
Structure deposition date
2021-03-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
89
Peptide accession
P62139
Residue number A
39
Residue number B
105
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 39 of Serine/threonine-protein phosphatase PP1-alpha 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 105 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
48
PDB code
7nzm
Structure name
cryo-em structure of pre-dephosphorylation complex of phosphorylated eif2alpha with trapped holophosphatase (pp1a_d64a/ppp1r15a/g- actin/dnase i)
Structure deposition date
2021-03-24
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
74
Peptide accession
P62139
Residue number A
245
Residue number B
291
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 245 of Serine/threonine-protein phosphatase PP1-alpha 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 291 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
39
PDB code
3e7b
Structure name
crystal structure of protein phosphatase-1 bound to the natural toxin inhibitor tautomycin
Structure deposition date
2008-08-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
P62136
Residue number A
171
Residue number B
291
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 171 of Serine/threonine-protein phosphatase PP1-alpha 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 291 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
38
PDB code
7nzm
Structure name
cryo-em structure of pre-dephosphorylation complex of phosphorylated eif2alpha with trapped holophosphatase (pp1a_d64a/ppp1r15a/g- actin/dnase i)
Structure deposition date
2021-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
12
% buried
89
Peptide accession
P62139
Residue number A
39
Residue number B
140
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 39 of Serine/threonine-protein phosphatase PP1-alpha 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 140 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
38
PDB code
7nzm
Structure name
cryo-em structure of pre-dephosphorylation complex of phosphorylated eif2alpha with trapped holophosphatase (pp1a_d64a/ppp1r15a/g- actin/dnase i)
Structure deposition date
2021-03-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
P62139
Residue number A
171
Residue number B
172
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 171 of Serine/threonine-protein phosphatase PP1-alpha 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 172 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
35
PDB code
4g9j
Structure name
protein ser/thr phosphatase-1 in complex with cell-permeable peptide
Structure deposition date
2012-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
70
Peptide accession
P62136
Residue number A
127
Residue number B
202
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 127 of Serine/threonine-protein phosphatase PP1-alpha 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 202 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
35
PDB code
7nzm
Structure name
cryo-em structure of pre-dephosphorylation complex of phosphorylated eif2alpha with trapped holophosphatase (pp1a_d64a/ppp1r15a/g- actin/dnase i)
Structure deposition date
2021-03-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
13
% buried
100
Peptide accession
P62139
Residue number A
105
Residue number B
140
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 105 of Serine/threonine-protein phosphatase PP1-alpha 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 140 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
29
PDB code
7nzm
Structure name
cryo-em structure of pre-dephosphorylation complex of phosphorylated eif2alpha with trapped holophosphatase (pp1a_d64a/ppp1r15a/g- actin/dnase i)
Structure deposition date
2021-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
100
Peptide accession
P62139
Residue number A
105
Residue number B
155
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 105 of Serine/threonine-protein phosphatase PP1-alpha 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 155 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
28
PDB code
6obs
Structure name
pp1 y134k
Structure deposition date
2019-03-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
101
Minimum pKa ?
13
% buried
100
Peptide accession
P62136
Residue number A
172
Residue number B
245
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 172 of Serine/threonine-protein phosphatase PP1-alpha 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 245 of Serine/threonine-protein phosphatase PP1-alpha 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-alpha 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 ?
20
PDB code
8dwl
Structure name
inhibitor-3:pp1 coexpressed complex
Structure deposition date
2022-08-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
100
Minimum pKa ?
13
% buried
100
Peptide accession
P62136
Residue number A
62
Residue number B
245
Peptide name
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Ligandability

Cysteine 62 of Serine/threonine-protein phosphatase PP1-alpha 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 245 of Serine/threonine-protein phosphatase PP1-alpha 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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