Histone deacetylase 6
Intermolecular
Cysteine 1120 and cysteine 1113
Cysteine 1148 and cysteine 1120
Cysteine 1145 and cysteine 1120
Cysteine 1120 and cysteine 1183
Cysteine 1186 and cysteine 1120
Cysteine 1148 and cysteine 1148
Intramolecular
Cysteine 1113 and cysteine 1186
Cysteine 1136 and cysteine 1153
Cysteine 1183 and cysteine 1186
Cysteine 1133 and cysteine 1136
More...Cysteine 1113 and cysteine 1183
Cysteine 1145 and cysteine 1148
Cysteine 1133 and cysteine 1153
Cysteine 493 and cysteine 572
Cysteine 572 and cysteine 578
Cysteine 618 and cysteine 621
Cysteine 493 and cysteine 578
Cysteine 539 and cysteine 587
3phd B 12 D 5
A redox-regulated disulphide may form between two units of Histone deacetylase 6 at cysteines 1120 and 1113 (12 and 5 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
3phd
Structure name
crystal structure of human hdac6 in complex with ubiquitin
Structure deposition date
2010-11-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
3
% buried
78
Peptide A name
Histone deacetylase 6
Peptide B name
Histone deacetylase 6
Peptide A accession
Q9UBN7
Peptide B accession
Q9UBN7
Peptide A residue number
1120
Peptide B residue number
1113
Ligandability
Cysteine 1120 of Histone deacetylase 6
Cysteine 1113 of Histone deacetylase 6
3phd B 40 D 12
A redox-regulated disulphide may form between two units of Histone deacetylase 6 at cysteines 1148 and 1120 (40 and 12 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3phd
Structure name
crystal structure of human hdac6 in complex with ubiquitin
Structure deposition date
2010-11-03
Thiol separation (Å)
5
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
100
Peptide A name
Histone deacetylase 6
Peptide B name
Histone deacetylase 6
Peptide A accession
Q9UBN7
Peptide B accession
Q9UBN7
Peptide A residue number
1148
Peptide B residue number
1120
Ligandability
Cysteine 1148 of Histone deacetylase 6
Cysteine 1120 of Histone deacetylase 6
3phd A 37 C 12
A redox-regulated disulphide may form between two units of Histone deacetylase 6 at cysteines 1145 and 1120 (37 and 12 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
3phd
Structure name
crystal structure of human hdac6 in complex with ubiquitin
Structure deposition date
2010-11-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
10
% buried
nan
Peptide A name
Histone deacetylase 6
Peptide B name
Histone deacetylase 6
Peptide A accession
Q9UBN7
Peptide B accession
Q9UBN7
Peptide A residue number
1145
Peptide B residue number
1120
Ligandability
Cysteine 1145 of Histone deacetylase 6
Cysteine 1120 of Histone deacetylase 6
3phd B 12 D 75
A redox-regulated disulphide may form between two units of Histone deacetylase 6 at cysteines 1120 and 1183 (12 and 75 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3phd
Structure name
crystal structure of human hdac6 in complex with ubiquitin
Structure deposition date
2010-11-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
80
Peptide A name
Histone deacetylase 6
Peptide B name
Histone deacetylase 6
Peptide A accession
Q9UBN7
Peptide B accession
Q9UBN7
Peptide A residue number
1120
Peptide B residue number
1183
Ligandability
Cysteine 1120 of Histone deacetylase 6
Cysteine 1183 of Histone deacetylase 6
3phd A 78 D 12
A redox-regulated disulphide may form between two units of Histone deacetylase 6 at cysteines 1186 and 1120 (78 and 12 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
3phd
Structure name
crystal structure of human hdac6 in complex with ubiquitin
Structure deposition date
2010-11-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
90
Peptide A name
Histone deacetylase 6
Peptide B name
Histone deacetylase 6
Peptide A accession
Q9UBN7
Peptide B accession
Q9UBN7
Peptide A residue number
1186
Peptide B residue number
1120
Ligandability
Cysteine 1186 of Histone deacetylase 6
Cysteine 1120 of Histone deacetylase 6
3phd B 40 D 40
A redox-regulated disulphide may form between two units of Histone deacetylase 6 at cysteines 1148 and 1148 (40 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
3phd
Structure name
crystal structure of human hdac6 in complex with ubiquitin
Structure deposition date
2010-11-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
14
% buried
89
Peptide A name
Histone deacetylase 6
Peptide B name
Histone deacetylase 6
Peptide A accession
Q9UBN7
Peptide B accession
Q9UBN7
Peptide A residue number
1148
Peptide B residue number
1148
Ligandability
3gv4 A 5 A 78
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 1113 and 1186 (5 and 78 respectively in this structure).
Details
Redox score ?
82
PDB code
3gv4
Structure name
crystal structure of human hdac6 zinc finger domain and ubiquitin c- terminal peptide rlrgg
Structure deposition date
2009-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
11
Peptide accession
Q9UBN7
Residue number A
1113
Residue number B
1186
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 1113 of Histone deacetylase 6
Cysteine 1186 of Histone deacetylase 6
3phd C 28 C 45
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 1136 and 1153 (28 and 45 respectively in this structure).
Details
Redox score ?
76
PDB code
3phd
Structure name
crystal structure of human hdac6 in complex with ubiquitin
Structure deposition date
2010-11-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
8
Peptide accession
Q9UBN7
Residue number A
1136
Residue number B
1153
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 1136 of Histone deacetylase 6
Cysteine 1153 of Histone deacetylase 6
6ce6 A 1183 A 1186
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 1183 and 1186.
Details
Redox score ?
75
PDB code
6ce6
Structure name
structure of hdac6 zinc-finger ubiquitin binding domain soaked with 3, 3'-(benzo[1,2-d:5,4-d']bis(thiazole)-2,6-diyl)dipropionic acid
Structure deposition date
2018-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UBN7
Residue number A
1183
Residue number B
1186
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 1183 of Histone deacetylase 6
Cysteine 1186 of Histone deacetylase 6
5kh9 A 1133 A 1136
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 1133 and 1136.
Details
Redox score ?
74
PDB code
5kh9
Structure name
crystal structure of a low occupancy fragment candidate (5-[(4- isopropylphenyl)amino]-6-methyl-1,2,4-triazin-3(2h)-one) bound in the ubiquitin binding pocket of the hdac6 zinc-finger domain
Structure deposition date
2016-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UBN7
Residue number A
1133
Residue number B
1136
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 1133 of Histone deacetylase 6
Cysteine 1136 of Histone deacetylase 6
6cea A 1113 A 1183
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 1113 and 1183.
Details
Redox score ?
74
PDB code
6cea
Structure name
crystal structure of fragment 3-(quinolin-2-yl)propanoic acid bound in the ubiquitin binding pocket of the hdac6 zinc-finger domain
Structure deposition date
2018-02-11
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UBN7
Residue number A
1113
Residue number B
1183
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 1113 of Histone deacetylase 6
Cysteine 1183 of Histone deacetylase 6
3gv4 A 37 A 40
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 1145 and 1148 (37 and 40 respectively in this structure).
Details
Redox score ?
72
PDB code
3gv4
Structure name
crystal structure of human hdac6 zinc finger domain and ubiquitin c- terminal peptide rlrgg
Structure deposition date
2009-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
8
% buried
50
Peptide accession
Q9UBN7
Residue number A
1145
Residue number B
1148
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 1145 of Histone deacetylase 6
Cysteine 1148 of Histone deacetylase 6
5b8d A 1133 A 1153
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 1133 and 1153.
Details
Redox score ?
72
PDB code
5b8d
Structure name
crystal structure of a low occupancy fragment candidate (n-(4-methyl- 1,3-thiazol-2-yl)propanamide) bound adjacent to the ubiquitin binding pocket of the hdac6 zinc-finger domain
Structure deposition date
2016-06-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UBN7
Residue number A
1133
Residue number B
1153
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 1133 of Histone deacetylase 6
Cysteine 1153 of Histone deacetylase 6
5edu B 493 B 572
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 493 and 572.
Details
Redox score ?
71
PDB code
5edu
Structure name
crystal structure of human histone deacetylase 6 catalytic domain 2 in complex with trichostatin a
Structure deposition date
2015-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
7
% buried
48
Peptide accession
Q9UBN7
Residue number A
493
Residue number B
572
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 493 of Histone deacetylase 6
Cysteine 572 of Histone deacetylase 6
5edu A 572 A 578
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 572 and 578. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5edu
Structure name
crystal structure of human histone deacetylase 6 catalytic domain 2 in complex with trichostatin a
Structure deposition date
2015-10-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
7
% buried
66
Peptide accession
Q9UBN7
Residue number A
572
Residue number B
578
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 572 of Histone deacetylase 6
Cysteine 578 of Histone deacetylase 6
5edu B 618 B 621
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 618 and 621. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5edu
Structure name
crystal structure of human histone deacetylase 6 catalytic domain 2 in complex with trichostatin a
Structure deposition date
2015-10-22
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
87
Peptide accession
Q9UBN7
Residue number A
618
Residue number B
621
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 618 of Histone deacetylase 6
Cysteine 621 of Histone deacetylase 6
5edu A 493 A 578
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 493 and 578. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
5edu
Structure name
crystal structure of human histone deacetylase 6 catalytic domain 2 in complex with trichostatin a
Structure deposition date
2015-10-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
50
Peptide accession
Q9UBN7
Residue number A
493
Residue number B
578
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 493 of Histone deacetylase 6
Cysteine 578 of Histone deacetylase 6
5edu B 539 B 587
A redox-regulated disulphide may form within Histone deacetylase 6 between cysteines 539 and 587. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
5edu
Structure name
crystal structure of human histone deacetylase 6 catalytic domain 2 in complex with trichostatin a
Structure deposition date
2015-10-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
94
Peptide accession
Q9UBN7
Residue number A
539
Residue number B
587
Peptide name
Histone deacetylase 6
Ligandability
Cysteine 539 of Histone deacetylase 6
Cysteine 587 of Histone deacetylase 6
If this tool was useful for finding a disulphide, please cite: