ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone deacetylase 1

Intramolecular
Cysteine 100 and cysteine 151
Cysteine 261 and cysteine 311
Cysteine 261 and cysteine 284
Cysteine 110 and cysteine 151
Cysteine 284 and cysteine 311
A redox-regulated disulphide may form within Histone deacetylase 1 between cysteines 100 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
4bkx
Structure name
the structure of hdac1 in complex with the dimeric elm2-sant domain of mta1 from the nurd complex
Structure deposition date
2013-04-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
92
Peptide accession
Q13547
Residue number A
100
Residue number B
151
Peptide name
Histone deacetylase 1

Ligandability

Cysteine 100 of Histone deacetylase 1

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 151 of Histone deacetylase 1

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 1 between cysteines 261 and 311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
5icn
Structure name
hdac1:mta1 in complex with inositol-6-phosphate and a novel peptide inhibitor based on histone h4
Structure deposition date
2016-02-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
15
% buried
100
Peptide accession
Q13547
Residue number A
261
Residue number B
311
Peptide name
Histone deacetylase 1

Ligandability

Cysteine 261 of Histone deacetylase 1

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 311 of Histone deacetylase 1

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 1 between cysteines 261 and 284. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
4bkx
Structure name
the structure of hdac1 in complex with the dimeric elm2-sant domain of mta1 from the nurd complex
Structure deposition date
2013-04-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
Q13547
Residue number A
261
Residue number B
284
Peptide name
Histone deacetylase 1

Ligandability

Cysteine 261 of Histone deacetylase 1

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 284 of Histone deacetylase 1

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 1 between cysteines 110 and 151. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
4bkx
Structure name
the structure of hdac1 in complex with the dimeric elm2-sant domain of mta1 from the nurd complex
Structure deposition date
2013-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
Q13547
Residue number A
110
Residue number B
151
Peptide name
Histone deacetylase 1

Ligandability

Cysteine 110 of Histone deacetylase 1

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 151 of Histone deacetylase 1

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 1 between cysteines 284 and 311. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
4bkx
Structure name
the structure of hdac1 in complex with the dimeric elm2-sant domain of mta1 from the nurd complex
Structure deposition date
2013-04-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
Q13547
Residue number A
284
Residue number B
311
Peptide name
Histone deacetylase 1

Ligandability

Cysteine 284 of Histone deacetylase 1

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 311 of Histone deacetylase 1

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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