ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Histone deacetylase 4

Intramolecular
Cysteine 667 and cysteine 751
Cysteine 667 and cysteine 669
Cysteine 669 and cysteine 751
Cysteine 698 and cysteine 700
Cysteine 700 and cysteine 777
Cysteine 952 and cysteine 988
A redox-regulated disulphide may form within Histone deacetylase 4 between cysteines 667 and 751 (23 and 107 respectively in this structure).

Details

Redox score ?
92
PDB code
2vqj
Structure name
structure of hdac4 catalytic domain bound to a trifluoromethylketone inhbitor
Structure deposition date
2008-03-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
6
% buried
0
Peptide accession
P56524
Residue number A
667
Residue number B
751
Peptide name
Histone deacetylase 4

Ligandability

Cysteine 667 of Histone deacetylase 4

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 751 of Histone deacetylase 4

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 4 between cysteines 667 and 669.

Details

Redox score ?
87
PDB code
4cbt
Structure name
design, synthesis, and biological evaluation of potent and selective class iia hdac inhibitors as a potential therapy for huntington's disease
Structure deposition date
2013-10-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
39
Minimum pKa ?
7
% buried
0
Peptide accession
P56524
Residue number A
667
Residue number B
669
Peptide name
Histone deacetylase 4

Ligandability

Cysteine 667 of Histone deacetylase 4

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 669 of Histone deacetylase 4

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 4 between cysteines 669 and 751.

Details

Redox score ?
86
PDB code
5a2s
Structure name
potent, selective and cns-penetrant tetrasubstituted cyclopropane class iia histone deacetylase (hdac) inhibitors
Structure deposition date
2015-05-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
7
% buried
0
Peptide accession
P56524
Residue number A
669
Residue number B
751
Peptide name
Histone deacetylase 4

Ligandability

Cysteine 669 of Histone deacetylase 4

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 751 of Histone deacetylase 4

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 4 between cysteines 698 and 700 (54 and 56 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2vqj
Structure name
structure of hdac4 catalytic domain bound to a trifluoromethylketone inhbitor
Structure deposition date
2008-03-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
56
Peptide accession
P56524
Residue number A
698
Residue number B
700
Peptide name
Histone deacetylase 4

Ligandability

Cysteine 698 of Histone deacetylase 4

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 700 of Histone deacetylase 4

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 4 between cysteines 700 and 777 (56 and 133 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
2vqj
Structure name
structure of hdac4 catalytic domain bound to a trifluoromethylketone inhbitor
Structure deposition date
2008-03-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
66
Peptide accession
P56524
Residue number A
700
Residue number B
777
Peptide name
Histone deacetylase 4

Ligandability

Cysteine 700 of Histone deacetylase 4

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 777 of Histone deacetylase 4

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 4 between cysteines 952 and 988. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
6fyz
Structure name
development and characterization of a cns-penetrant benzhydryl hydroxamic acid class iia histone deacetylase inhibitor
Structure deposition date
2018-03-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
P56524
Residue number A
952
Residue number B
988
Peptide name
Histone deacetylase 4

Ligandability

Cysteine 952 of Histone deacetylase 4

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 988 of Histone deacetylase 4

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.

If this tool was useful for finding a disulphide, please cite: