ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Intramolecular
Cysteine 148 and cysteine 174
Cysteine 310 and cysteine 317 L
Cysteine 310 and cysteine 329 L
Cysteine 504 and cysteine 512
Cysteine 447 and cysteine 504
A redox-regulated disulphide may form within Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform between cysteines 148 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2nym
Structure name
crystal structure of protein phosphatase 2a (pp2a) with c-terminus truncated catalytic subunit
Structure deposition date
2006-11-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
Q96DH3
Residue number A
148
Residue number B
174
Peptide name
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Ligandability

Cysteine 148 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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 65 kDa regulatory subunit A alpha isoform

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 65 kDa regulatory subunit A alpha isoform between cysteines 310 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4i5l
Structure name
structural mechanism of trimeric pp2a holoenzyme involving pr70: insight for cdc6 dephosphorylation
Structure deposition date
2012-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
56
Peptide accession
P30153
Residue number A
310
Residue number B
317
Peptide name
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Ligandability

Cysteine 310 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 317 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform between cysteines 310 and 329. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5w0w
Structure name
crystal structure of protein phosphatase 2a bound to tiprl
Structure deposition date
2017-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
71
Peptide accession
P30153
Residue number A
310
Residue number B
329
Peptide name
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Ligandability

Cysteine 310 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 329 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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.

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 65 kDa regulatory subunit A alpha isoform between cysteines 504 and 512. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6nts
Structure name
protein phosphatase 2a (aalpha-b56alpha-calpha) holoenzyme in complex with a small molecule activator of pp2a (smap)
Structure deposition date
2019-01-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
74
Peptide accession
P30153
Residue number A
504
Residue number B
512
Peptide name
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Ligandability

Cysteine 504 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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 512 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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 65 kDa regulatory subunit A alpha isoform between cysteines 447 and 504. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6iur
Structure name
a phosphatase complex strn3-pp2aa
Structure deposition date
2018-11-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
P30153
Residue number A
447
Residue number B
504
Peptide name
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Ligandability

Cysteine 447 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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 504 of Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

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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