ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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SH3 domain-containing protein

Intermolecular
Cysteine 246 and cysteine 246
Intramolecular
Cysteine 355 and cysteine 385
Cysteine 413 and cysteine 415
Cysteine 385 and cysteine 415
Cysteine 385 and cysteine 413
A redox-regulated disulphide may form between two units of SH3 domain-containing protein at cysteines 246 and 246 (419 and 419 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
3d4i
Structure name
crystal structure of the 2h-phosphatase domain of sts-2
Structure deposition date
2008-05-14
Thiol separation (Å)
5
Half-sphere exposure sum ?
92
Minimum pKa ?
15
% buried
100
Peptide A name
SH3 domain-containing protein
Peptide B name
SH3 domain-containing protein
Peptide A accession
Q8BX41
Peptide B accession
Q8BX41
Peptide A residue number
246
Peptide B residue number
246

Ligandability

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 domain-containing protein between cysteines 355 and 385 (528 and 558 respectively in this structure).

Details

Redox score ?
67
PDB code
3d6a
Structure name
crystal structure of the 2h-phosphatase domain of sts-2 in complex with tungstate
Structure deposition date
2008-05-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BX41
Residue number A
355
Residue number B
385
Peptide name
SH3 domain-containing protein

Ligandability

Cysteine 355 of SH3 domain-containing protein

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 385 of SH3 domain-containing protein

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 domain-containing protein between cysteines 413 and 415 (586 and 588 respectively in this structure).

Details

Redox score ?
63
PDB code
3d6a
Structure name
crystal structure of the 2h-phosphatase domain of sts-2 in complex with tungstate
Structure deposition date
2008-05-19
Thiol separation (Å)
5
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BX41
Residue number A
413
Residue number B
415
Peptide name
SH3 domain-containing protein

Ligandability

Cysteine 413 of SH3 domain-containing protein

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 415 of SH3 domain-containing protein

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 domain-containing protein between cysteines 385 and 415 (558 and 588 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3d6a
Structure name
crystal structure of the 2h-phosphatase domain of sts-2 in complex with tungstate
Structure deposition date
2008-05-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BX41
Residue number A
385
Residue number B
415
Peptide name
SH3 domain-containing protein

Ligandability

Cysteine 385 of SH3 domain-containing protein

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 415 of SH3 domain-containing protein

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 domain-containing protein between cysteines 385 and 413 (558 and 586 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
3d4i
Structure name
crystal structure of the 2h-phosphatase domain of sts-2
Structure deposition date
2008-05-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
94
Minimum pKa ?
16
% buried
100
Peptide accession
Q8BX41
Residue number A
385
Residue number B
413
Peptide name
SH3 domain-containing protein

Ligandability

Cysteine 385 of SH3 domain-containing protein

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 413 of SH3 domain-containing protein

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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