ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Histone deacetylase 8

Intermolecular
Cysteine 275 and cysteine 275
Intramolecular
Cysteine 244 and cysteine 287
Cysteine 125 and cysteine 131
Cysteine 102 and cysteine 153
Cysteine 275 and cysteine 352
A redox-regulated disulphide may form between two units of Histone deacetylase 8 at cysteines 275 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
3rqd
Structure name
ideal thiolate-zinc coordination geometry in depsipeptide binding to histone deacetylase 8
Structure deposition date
2011-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
100
Peptide A name
Histone deacetylase 8
Peptide B name
Histone deacetylase 8
Peptide A accession
Q9BY41
Peptide B accession
Q9BY41
Peptide A residue number
275
Peptide B residue number
275

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 Histone deacetylase 8 between cysteines 244 and 287.

Details

Redox score ?
73
PDB code
3mz3
Structure name
crystal structure of co2+ hdac8 complexed with m344
Structure deposition date
2010-05-11
Thiol separation (Å)
3
Half-sphere exposure sum ?
79
Minimum pKa ?
9
% buried
100
Peptide accession
Q9BY41
Residue number A
244
Residue number B
287
Peptide name
Histone deacetylase 8

Ligandability

Cysteine 244 of Histone deacetylase 8

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 287 of Histone deacetylase 8

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 8 between cysteines 125 and 131.

Details

Redox score ?
70
PDB code
3ezt
Structure name
crystal structure analysis of human hdac8 d101e variant
Structure deposition date
2008-10-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
53
Peptide accession
Q9BY41
Residue number A
125
Residue number B
131
Peptide name
Histone deacetylase 8

Ligandability

Cysteine 125 of Histone deacetylase 8

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 131 of Histone deacetylase 8

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 8 between cysteines 102 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
3f06
Structure name
crystal structure analysis of human hdac8 d101a variant
Structure deposition date
2008-10-24
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
88
Peptide accession
Q9BY41
Residue number A
102
Residue number B
153
Peptide name
Histone deacetylase 8

Ligandability

Cysteine 102 of Histone deacetylase 8

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 153 of Histone deacetylase 8

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 8 between cysteines 275 and 352. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3f0r
Structure name
crystal structure analysis of human hdac8 complexed with trichostatin a in a new monoclinic crystal form
Structure deposition date
2008-10-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
4
Peptide accession
Q9BY41
Residue number A
275
Residue number B
352
Peptide name
Histone deacetylase 8

Ligandability

Cysteine 275 of Histone deacetylase 8

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 352 of Histone deacetylase 8

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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