ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Phosducin-like protein 2

Intramolecular
Cysteine 125 and cysteine 160
Cysteine 152 and cysteine 160
Cysteine 125 and cysteine 182
Cysteine 160 and cysteine 182
A redox-regulated disulphide may form within Phosducin-like protein 2 between cysteines 125 and 160 (45 and 80 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2dbc
Structure name
solution structure of the thioredoxin-like domain of phosducin-like protein 2(pdcl2)
Structure deposition date
2005-12-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
10
% buried
22
Peptide accession
Q9DA99
Residue number A
125
Residue number B
160
Peptide name
Phosducin-like protein 2

Ligandability

Cysteine 125 of Phosducin-like protein 2

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 160 of Phosducin-like protein 2

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 Phosducin-like protein 2 between cysteines 152 and 160 (72 and 80 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2dbc
Structure name
solution structure of the thioredoxin-like domain of phosducin-like protein 2(pdcl2)
Structure deposition date
2005-12-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
43
Minimum pKa ?
10
% buried
12
Peptide accession
Q9DA99
Residue number A
152
Residue number B
160
Peptide name
Phosducin-like protein 2

Ligandability

Cysteine 152 of Phosducin-like protein 2

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 160 of Phosducin-like protein 2

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 Phosducin-like protein 2 between cysteines 125 and 182. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3evi
Structure name
crystal structure of the thioredoxin-fold domain of human phosducin- like protein 2
Structure deposition date
2008-10-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
66
Peptide accession
Q8N4E4
Residue number A
125
Residue number B
182
Peptide name
Phosducin-like protein 2

Ligandability

Cysteine 125 of Phosducin-like protein 2

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 Phosducin-like protein 2

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 Phosducin-like protein 2 between cysteines 160 and 182 (80 and 102 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
2dbc
Structure name
solution structure of the thioredoxin-like domain of phosducin-like protein 2(pdcl2)
Structure deposition date
2005-12-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
40
Peptide accession
Q9DA99
Residue number A
160
Residue number B
182
Peptide name
Phosducin-like protein 2

Ligandability

Cysteine 160 of Phosducin-like protein 2

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 Phosducin-like protein 2

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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