ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Switch-associated protein 70

Intramolecular
Cysteine 260 and cysteine 279
Cysteine 261 and cysteine 279 L
Cysteine 260 and cysteine 261 L
A redox-regulated disulphide may form within Switch-associated protein 70 between cysteines 260 and 279 (57 and 76 respectively in this structure).

Details

Redox score ?
87
PDB code
2dn6
Structure name
solution structure of the ph domain of kiaa0640 protein from human
Structure deposition date
2006-04-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UH65
Residue number A
260
Residue number B
279
Peptide name
Switch-associated protein 70

Ligandability

Cysteine 260 of Switch-associated protein 70

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 279 of Switch-associated protein 70

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 Switch-associated protein 70 between cysteines 261 and 279 (58 and 76 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2dn6
Structure name
solution structure of the ph domain of kiaa0640 protein from human
Structure deposition date
2006-04-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UH65
Residue number A
261
Residue number B
279
Peptide name
Switch-associated protein 70

Ligandability

Cysteine 261 of Switch-associated protein 70

Not ligandable in the dataset of Yang et al.

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 279 of Switch-associated protein 70

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 Switch-associated protein 70 between cysteines 260 and 261 (57 and 58 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
2dn6
Structure name
solution structure of the ph domain of kiaa0640 protein from human
Structure deposition date
2006-04-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UH65
Residue number A
260
Residue number B
261
Peptide name
Switch-associated protein 70

Ligandability

Cysteine 260 of Switch-associated protein 70

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 261 of Switch-associated protein 70

Not ligandable in the dataset of Yang et al.

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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