ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone deacetylase complex subunit SAP30L

Intramolecular
Cysteine 29 and cysteine 38
Cysteine 29 and cysteine 74
Cysteine 38 and cysteine 74
Cysteine 29 and cysteine 30
Cysteine 30 and cysteine 38
Cysteine 30 and cysteine 74
A redox-regulated disulphide may form within Histone deacetylase complex subunit SAP30L between cysteines 29 and 38.

Details

Redox score ?
85
PDB code
2n1u
Structure name
structure of sap30l corepressor protein
Structure deposition date
2015-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
6
% buried
28
Peptide accession
Q9HAJ7
Residue number A
29
Residue number B
38
Peptide name
Histone deacetylase complex subunit SAP30L

Ligandability

Cysteine 29 of Histone deacetylase complex subunit SAP30L

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 38 of Histone deacetylase complex subunit SAP30L

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 SAP30L between cysteines 29 and 74.

Details

Redox score ?
82
PDB code
2n1u
Structure name
structure of sap30l corepressor protein
Structure deposition date
2015-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
29
Peptide accession
Q9HAJ7
Residue number A
29
Residue number B
74
Peptide name
Histone deacetylase complex subunit SAP30L

Ligandability

Cysteine 29 of Histone deacetylase complex subunit SAP30L

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 74 of Histone deacetylase complex subunit SAP30L

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 SAP30L between cysteines 38 and 74.

Details

Redox score ?
81
PDB code
2n1u
Structure name
structure of sap30l corepressor protein
Structure deposition date
2015-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
22
Peptide accession
Q9HAJ7
Residue number A
38
Residue number B
74
Peptide name
Histone deacetylase complex subunit SAP30L

Ligandability

Cysteine 38 of Histone deacetylase complex subunit SAP30L

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 74 of Histone deacetylase complex subunit SAP30L

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 SAP30L between cysteines 29 and 30.

Details

Redox score ?
69
PDB code
2n1u
Structure name
structure of sap30l corepressor protein
Structure deposition date
2015-04-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
6
% buried
28
Peptide accession
Q9HAJ7
Residue number A
29
Residue number B
30
Peptide name
Histone deacetylase complex subunit SAP30L

Ligandability

Cysteine 29 of Histone deacetylase complex subunit SAP30L

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 30 of Histone deacetylase complex subunit SAP30L

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 SAP30L between cysteines 30 and 38. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
2n1u
Structure name
structure of sap30l corepressor protein
Structure deposition date
2015-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
20
Peptide accession
Q9HAJ7
Residue number A
30
Residue number B
38
Peptide name
Histone deacetylase complex subunit SAP30L

Ligandability

Cysteine 30 of Histone deacetylase complex subunit SAP30L

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 38 of Histone deacetylase complex subunit SAP30L

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 SAP30L between cysteines 30 and 74. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
2n1u
Structure name
structure of sap30l corepressor protein
Structure deposition date
2015-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
21
Peptide accession
Q9HAJ7
Residue number A
30
Residue number B
74
Peptide name
Histone deacetylase complex subunit SAP30L

Ligandability

Cysteine 30 of Histone deacetylase complex subunit SAP30L

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 74 of Histone deacetylase complex subunit SAP30L

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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