ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Profilin-2

Intramolecular
Cysteine 16 and cysteine 17
Cysteine 13 and cysteine 16
Cysteine 13 and cysteine 17
A redox-regulated disulphide may form within Profilin-2 between cysteines 16 and 17 (15 and 16 respectively in this structure).

Details

Redox score ?
86
PDB code
2vk3
Structure name
crystal structure of rat profilin 2a
Structure deposition date
2007-12-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9EPC6
Residue number A
16
Residue number B
17
Peptide name
Profilin-2

Ligandability

Cysteine 16 of Profilin-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 17 of Profilin-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 Profilin-2 between cysteines 13 and 16 (12 and 15 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
2v8f
Structure name
mouse profilin iia in complex with a double repeat from the fh1 domain of mdia1
Structure deposition date
2007-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
4
Peptide accession
Q3V171
Residue number A
13
Residue number B
16
Peptide name
Profilin-2

Ligandability

Cysteine 13 of Profilin-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 16 of Profilin-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 Profilin-2 between cysteines 13 and 17 (12 and 16 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2v8c
Structure name
mouse profilin iia in complex with the proline-rich domain of vasp
Structure deposition date
2007-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
32
Peptide accession
Q3V171
Residue number A
13
Residue number B
17
Peptide name
Profilin-2

Ligandability

Cysteine 13 of Profilin-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 17 of Profilin-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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