ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone deacetylase complex subunit SAP30

Intramolecular
Cysteine 76 and cysteine 112
Cysteine 67 and cysteine 112
Cysteine 67 and cysteine 76
Cysteine 67 and cysteine 68
Cysteine 68 and cysteine 112
Cysteine 68 and cysteine 76
A redox-regulated disulphide may form within Histone deacetylase complex subunit SAP30 between cysteines 76 and 112.

Details

Redox score ?
82
PDB code
2kdp
Structure name
solution structure of the sap30 zinc finger motif
Structure deposition date
2009-01-14
Thiol separation (Å)
3
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
21
Peptide accession
O75446
Residue number A
76
Residue number B
112
Peptide name
Histone deacetylase complex subunit SAP30

Ligandability

Cysteine 76 of Histone deacetylase complex subunit SAP30

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 112 of Histone deacetylase complex subunit SAP30

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 Histone deacetylase complex subunit SAP30 between cysteines 67 and 112.

Details

Redox score ?
80
PDB code
2kdp
Structure name
solution structure of the sap30 zinc finger motif
Structure deposition date
2009-01-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
30
Peptide accession
O75446
Residue number A
67
Residue number B
112
Peptide name
Histone deacetylase complex subunit SAP30

Ligandability

Cysteine 67 of Histone deacetylase complex subunit SAP30

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 112 of Histone deacetylase complex subunit SAP30

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 Histone deacetylase complex subunit SAP30 between cysteines 67 and 76.

Details

Redox score ?
78
PDB code
2kdp
Structure name
solution structure of the sap30 zinc finger motif
Structure deposition date
2009-01-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
26
Peptide accession
O75446
Residue number A
67
Residue number B
76
Peptide name
Histone deacetylase complex subunit SAP30

Ligandability

Cysteine 67 of Histone deacetylase complex subunit SAP30

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 76 of Histone deacetylase complex subunit SAP30

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 Histone deacetylase complex subunit SAP30 between cysteines 67 and 68.

Details

Redox score ?
63
PDB code
2kdp
Structure name
solution structure of the sap30 zinc finger motif
Structure deposition date
2009-01-14
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
9
% buried
30
Peptide accession
O75446
Residue number A
67
Residue number B
68
Peptide name
Histone deacetylase complex subunit SAP30

Ligandability

Cysteine 67 of Histone deacetylase complex subunit SAP30

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 68 of Histone deacetylase complex subunit SAP30

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 Histone deacetylase complex subunit SAP30 between cysteines 68 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2kdp
Structure name
solution structure of the sap30 zinc finger motif
Structure deposition date
2009-01-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
8
% buried
26
Peptide accession
O75446
Residue number A
68
Residue number B
112
Peptide name
Histone deacetylase complex subunit SAP30

Ligandability

Cysteine 68 of Histone deacetylase complex subunit SAP30

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 112 of Histone deacetylase complex subunit SAP30

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 Histone deacetylase complex subunit SAP30 between cysteines 68 and 76. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2kdp
Structure name
solution structure of the sap30 zinc finger motif
Structure deposition date
2009-01-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
21
Peptide accession
O75446
Residue number A
68
Residue number B
76
Peptide name
Histone deacetylase complex subunit SAP30

Ligandability

Cysteine 68 of Histone deacetylase complex subunit SAP30

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 76 of Histone deacetylase complex subunit SAP30

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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