Histone deacetylase 3
Intramolecular
Cysteine 94 and cysteine 145
Cysteine 123 and cysteine 251 L
Cysteine 94 and cysteine 104
Cysteine 256 and cysteine 306
Cysteine 256 and cysteine 279 L
Cysteine 279 and cysteine 306 L
Cysteine 104 and cysteine 145
4a69 A 94 A 145
A redox-regulated disulphide may form within Histone deacetylase 3 between cysteines 94 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
4a69
Structure name
structure of hdac3 bound to corepressor and inositol tetraphosphate
Structure deposition date
2011-11-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
O15379
Residue number A
94
Residue number B
145
Peptide name
Histone deacetylase 3
Ligandability
Cysteine 94 of Histone deacetylase 3
Cysteine 145 of Histone deacetylase 3
4a69 B 123 B 251
A redox-regulated disulphide may form within Histone deacetylase 3 between cysteines 123 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
4a69
Structure name
structure of hdac3 bound to corepressor and inositol tetraphosphate
Structure deposition date
2011-11-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
96
Peptide accession
O15379
Residue number A
123
Residue number B
251
Peptide name
Histone deacetylase 3
Ligandability
Cysteine 123 of Histone deacetylase 3
Cysteine 251 of Histone deacetylase 3
4a69 A 94 A 104
A redox-regulated disulphide may form within Histone deacetylase 3 between cysteines 94 and 104. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
4a69
Structure name
structure of hdac3 bound to corepressor and inositol tetraphosphate
Structure deposition date
2011-11-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
13
% buried
100
Peptide accession
O15379
Residue number A
94
Residue number B
104
Peptide name
Histone deacetylase 3
Ligandability
Cysteine 94 of Histone deacetylase 3
Cysteine 104 of Histone deacetylase 3
4a69 B 256 B 306
A redox-regulated disulphide may form within Histone deacetylase 3 between cysteines 256 and 306. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
4a69
Structure name
structure of hdac3 bound to corepressor and inositol tetraphosphate
Structure deposition date
2011-11-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
15
% buried
100
Peptide accession
O15379
Residue number A
256
Residue number B
306
Peptide name
Histone deacetylase 3
Ligandability
Cysteine 256 of Histone deacetylase 3
Cysteine 306 of Histone deacetylase 3
4a69 A 256 A 279
A redox-regulated disulphide may form within Histone deacetylase 3 between cysteines 256 and 279. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
4a69
Structure name
structure of hdac3 bound to corepressor and inositol tetraphosphate
Structure deposition date
2011-11-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
O15379
Residue number A
256
Residue number B
279
Peptide name
Histone deacetylase 3
Ligandability
Cysteine 256 of Histone deacetylase 3
Cysteine 279 of Histone deacetylase 3
4a69 B 279 B 306
A redox-regulated disulphide may form within Histone deacetylase 3 between cysteines 279 and 306. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
25
PDB code
4a69
Structure name
structure of hdac3 bound to corepressor and inositol tetraphosphate
Structure deposition date
2011-11-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
O15379
Residue number A
279
Residue number B
306
Peptide name
Histone deacetylase 3
Ligandability
Cysteine 279 of Histone deacetylase 3
Cysteine 306 of Histone deacetylase 3
4a69 A 104 A 145
A redox-regulated disulphide may form within Histone deacetylase 3 between cysteines 104 and 145. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
4a69
Structure name
structure of hdac3 bound to corepressor and inositol tetraphosphate
Structure deposition date
2011-11-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
100
Peptide accession
O15379
Residue number A
104
Residue number B
145
Peptide name
Histone deacetylase 3
Ligandability
Cysteine 104 of Histone deacetylase 3
Cysteine 145 of Histone deacetylase 3
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