ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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SH3 and cysteine-rich domain-containing protein 2

Intramolecular
Cysteine 358 and cysteine 359
Cysteine 358 and cysteine 379
Cysteine 359 and cysteine 379
A redox-regulated disulphide may form within SH3 and cysteine-rich domain-containing protein 2 between cysteines 358 and 359.

Details

Redox score ?
63
PDB code
6b27
Structure name
crystal structure of human stac2 tandem sh3 domains (296-411) in complex with a cav1
Structure deposition date
2017-09-19
Thiol separation (Å)
6
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
40
Peptide accession
Q6ZMT1
Residue number A
358
Residue number B
359
Peptide name
SH3 and cysteine-rich domain-containing protein 2

Ligandability

Cysteine 358 of SH3 and cysteine-rich domain-containing 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 359 of SH3 and cysteine-rich domain-containing 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 SH3 and cysteine-rich domain-containing protein 2 between cysteines 358 and 379. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
6b28
Structure name
crystal structure of human stac2 tandem sh3 domains q347i (296-411)
Structure deposition date
2017-09-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
36
Peptide accession
Q6ZMT1
Residue number A
358
Residue number B
379
Peptide name
SH3 and cysteine-rich domain-containing protein 2

Ligandability

Cysteine 358 of SH3 and cysteine-rich domain-containing 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 379 of SH3 and cysteine-rich domain-containing 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 SH3 and cysteine-rich domain-containing protein 2 between cysteines 359 and 379. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6b27
Structure name
crystal structure of human stac2 tandem sh3 domains (296-411) in complex with a cav1
Structure deposition date
2017-09-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
47
Peptide accession
Q6ZMT1
Residue number A
359
Residue number B
379
Peptide name
SH3 and cysteine-rich domain-containing protein 2

Ligandability

Cysteine 359 of SH3 and cysteine-rich domain-containing 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 379 of SH3 and cysteine-rich domain-containing 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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