Histone deacetylase 7
Intramolecular
Cysteine 535 and cysteine 618
Cysteine 533 and cysteine 535
Cysteine 533 and cysteine 618
Cysteine 564 and cysteine 566
Cysteine 819 and cysteine 855
3c10 A 535 A 618
A redox-regulated disulphide may form within Histone deacetylase 7 between cysteines 535 and 618.
Details
Redox score ?
85
PDB code
3c10
Structure name
crystal structure of catalytic domain of human histone deacetylase hdac7 in complex with trichostatin a (tsa)
Structure deposition date
2008-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
0
Peptide accession
Q8WUI4
Residue number A
535
Residue number B
618
Peptide name
Histone deacetylase 7
Ligandability
Cysteine 535 of Histone deacetylase 7
Cysteine 618 of Histone deacetylase 7
3c0z B 533 B 535
A redox-regulated disulphide may form within Histone deacetylase 7 between cysteines 533 and 535.
Details
Redox score ?
85
PDB code
3c0z
Structure name
crystal structure of catalytic domain of human histone deacetylase hdac7 in complex with saha
Structure deposition date
2008-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
6
% buried
8
Peptide accession
Q8WUI4
Residue number A
533
Residue number B
535
Peptide name
Histone deacetylase 7
Ligandability
Cysteine 533 of Histone deacetylase 7
Cysteine 535 of Histone deacetylase 7
3c10 B 533 B 618
A redox-regulated disulphide may form within Histone deacetylase 7 between cysteines 533 and 618.
Details
Redox score ?
81
PDB code
3c10
Structure name
crystal structure of catalytic domain of human histone deacetylase hdac7 in complex with trichostatin a (tsa)
Structure deposition date
2008-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
10
Peptide accession
Q8WUI4
Residue number A
533
Residue number B
618
Peptide name
Histone deacetylase 7
Ligandability
Cysteine 533 of Histone deacetylase 7
Cysteine 618 of Histone deacetylase 7
3c0y B 564 B 566
A redox-regulated disulphide may form within Histone deacetylase 7 between cysteines 564 and 566. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
3c0y
Structure name
crystal structure of catalytic domain of human histone deacetylase hdac7
Structure deposition date
2008-01-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
88
Peptide accession
Q8WUI4
Residue number A
564
Residue number B
566
Peptide name
Histone deacetylase 7
Ligandability
Cysteine 564 of Histone deacetylase 7
Cysteine 566 of Histone deacetylase 7
3c0z A 819 A 855
A redox-regulated disulphide may form within Histone deacetylase 7 between cysteines 819 and 855. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
26
PDB code
3c0z
Structure name
crystal structure of catalytic domain of human histone deacetylase hdac7 in complex with saha
Structure deposition date
2008-01-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
Q8WUI4
Residue number A
819
Residue number B
855
Peptide name
Histone deacetylase 7
Ligandability
Cysteine 819 of Histone deacetylase 7
Cysteine 855 of Histone deacetylase 7
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