Histone deacetylase 2
Intramolecular
Cysteine 101 and cysteine 152
Cysteine 262 and cysteine 312 L
Cysteine 262 and cysteine 285
Cysteine 101 and cysteine 111
Cysteine 285 and cysteine 312 L
Cysteine 111 and cysteine 152
7kbh B 101 B 152
A redox-regulated disulphide may form within Histone deacetylase 2 between cysteines 101 and 152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
7kbh
Structure name
structure of human hdac2 in complex with a 2-substituted benzamide inhibitor (compound 16)
Structure deposition date
2020-10-02
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
98
Peptide accession
Q92769
Residue number A
101
Residue number B
152
Peptide name
Histone deacetylase 2
Ligandability
Cysteine 101 of Histone deacetylase 2
Cysteine 152 of Histone deacetylase 2
6whz A 266 A 316
A redox-regulated disulphide may form within Histone deacetylase 2 between cysteines 262 and 312 (266 and 316 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
6whz
Structure name
histone deacetylases complex with peptide macrocycles
Structure deposition date
2020-04-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
15
% buried
100
Peptide accession
Q92769
Residue number A
262
Residue number B
312
Peptide name
Histone deacetylase 2
Ligandability
Cysteine 262 of Histone deacetylase 2
Cysteine 312 of Histone deacetylase 2
7kbh C 263 C 286
A redox-regulated disulphide may form within Histone deacetylase 2 between cysteines 262 and 285 (263 and 286 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
7kbh
Structure name
structure of human hdac2 in complex with a 2-substituted benzamide inhibitor (compound 16)
Structure deposition date
2020-10-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
Q92769
Residue number A
262
Residue number B
285
Peptide name
Histone deacetylase 2
Ligandability
Cysteine 262 of Histone deacetylase 2
Cysteine 285 of Histone deacetylase 2
6who A 105 A 115
A redox-regulated disulphide may form within Histone deacetylase 2 between cysteines 101 and 111 (105 and 115 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
6who
Structure name
histone deacetylases complex with peptide macrocycles
Structure deposition date
2020-04-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
100
Peptide accession
Q92769
Residue number A
101
Residue number B
111
Peptide name
Histone deacetylase 2
Ligandability
Cysteine 101 of Histone deacetylase 2
Cysteine 111 of Histone deacetylase 2
3max C 289 C 316
A redox-regulated disulphide may form within Histone deacetylase 2 between cysteines 285 and 312 (289 and 316 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
3max
Structure name
crystal structure of human hdac2 complexed with an n-(2-aminophenyl) benzamide
Structure deposition date
2010-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
Q92769
Residue number A
285
Residue number B
312
Peptide name
Histone deacetylase 2
Ligandability
Cysteine 285 of Histone deacetylase 2
Cysteine 312 of Histone deacetylase 2
5ix0 C 115 C 156
A redox-regulated disulphide may form within Histone deacetylase 2 between cysteines 111 and 152 (115 and 156 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
5ix0
Structure name
hdac2 with ligand brd7232
Structure deposition date
2016-03-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
82
Minimum pKa ?
13
% buried
100
Peptide accession
Q92769
Residue number A
111
Residue number B
152
Peptide name
Histone deacetylase 2
Ligandability
Cysteine 111 of Histone deacetylase 2
Cysteine 152 of Histone deacetylase 2
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