ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Pleckstrin

Intermolecular
Cysteine 295 and cysteine 250
Intramolecular
Cysteine 155 and cysteine 226
Cysteine 155 and cysteine 160
A redox-regulated disulphide may form between two units of Pleckstrin at cysteines 295 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
2i5c
Structure name
crystal structure of the c-terminal ph domain of pleckstrin in complex with d-myo-ins(1,2,3,4,5)p5
Structure deposition date
2006-08-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
88
Peptide A name
Pleckstrin
Peptide B name
Pleckstrin
Peptide A accession
P08567
Peptide B accession
P08567
Peptide A residue number
295
Peptide B residue number
250

Ligandability

Cysteine 295 of Pleckstrin

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 250 of Pleckstrin

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 Pleckstrin between cysteines 155 and 226 (47 and 118 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
2cso
Structure name
solution structure of the dep domain of human pleckstrin
Structure deposition date
2005-05-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
31
Peptide accession
P08567
Residue number A
155
Residue number B
226
Peptide name
Pleckstrin

Ligandability

Cysteine 155 of Pleckstrin

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 226 of Pleckstrin

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 Pleckstrin between cysteines 155 and 160 (47 and 52 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
2cso
Structure name
solution structure of the dep domain of human pleckstrin
Structure deposition date
2005-05-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
52
Peptide accession
P08567
Residue number A
155
Residue number B
160
Peptide name
Pleckstrin

Ligandability

Cysteine 155 of Pleckstrin

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 Pleckstrin

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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