ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Bromodomain adjacent to zinc finger domain protein 2A

Intramolecular
Cysteine 1694 and cysteine 1720
Cysteine 1694 and cysteine 1723
Cysteine 1694 and cysteine 1697
Cysteine 1679 and cysteine 1705
Cysteine 1679 and cysteine 1682
Cysteine 1697 and cysteine 1723
Cysteine 1682 and cysteine 1705
Cysteine 1679 and cysteine 1701
Cysteine 1720 and cysteine 1723
Cysteine 1697 and cysteine 1720
More...
Cysteine 1701 and cysteine 1705
Cysteine 1682 and cysteine 1701
Cysteine 1701 and cysteine 1720
A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1694 and 1720.

Details

Redox score ?
90
PDB code
6fkp
Structure name
crystal structure of baz2a phd zinc finger in complex with h3 10-mer aa mutant peptide
Structure deposition date
2018-01-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
0
% buried
64
Peptide accession
Q9UIF9
Residue number A
1694
Residue number B
1720
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1694 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1720 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1694 and 1723.

Details

Redox score ?
89
PDB code
5t8r
Structure name
crystal structure of human baz2a phd zinc finger in complex with unmodified h3 10-mer
Structure deposition date
2016-09-08
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
3
% buried
32
Peptide accession
Q9UIF9
Residue number A
1694
Residue number B
1723
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1694 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1723 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1694 and 1697.

Details

Redox score ?
85
PDB code
6fi0
Structure name
crystal structure of baz2a phd zinc finger in complex with fr 19
Structure deposition date
2018-01-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
6
% buried
10
Peptide accession
Q9UIF9
Residue number A
1694
Residue number B
1697
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1694 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1697 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1679 and 1705.

Details

Redox score ?
85
PDB code
6fhu
Structure name
crystal structure of baz2a phd zinc finger in complex with h3 3-mer peptide
Structure deposition date
2018-01-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
22
Peptide accession
Q9UIF9
Residue number A
1679
Residue number B
1705
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1679 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1705 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1679 and 1682.

Details

Redox score ?
84
PDB code
4q6f
Structure name
crystal structure of human baz2a phd zinc finger in complex with unmodified h3k4 histone peptide
Structure deposition date
2014-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
6
% buried
22
Peptide accession
Q9UIF9
Residue number A
1679
Residue number B
1682
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1679 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1682 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1697 and 1723.

Details

Redox score ?
78
PDB code
5t8r
Structure name
crystal structure of human baz2a phd zinc finger in complex with unmodified h3 10-mer
Structure deposition date
2016-09-08
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
24
Peptide accession
Q9UIF9
Residue number A
1697
Residue number B
1723
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1697 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1723 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1682 and 1705.

Details

Redox score ?
78
PDB code
6fap
Structure name
crystal structure of human baz2a phd zinc finger in complex with fr23
Structure deposition date
2017-12-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
6
Peptide accession
Q9UIF9
Residue number A
1682
Residue number B
1705
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1682 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1705 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1679 and 1701.

Details

Redox score ?
75
PDB code
4q6f
Structure name
crystal structure of human baz2a phd zinc finger in complex with unmodified h3k4 histone peptide
Structure deposition date
2014-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
6
% buried
60
Peptide accession
Q9UIF9
Residue number A
1679
Residue number B
1701
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1679 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1701 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1720 and 1723.

Details

Redox score ?
70
PDB code
6fi0
Structure name
crystal structure of baz2a phd zinc finger in complex with fr 19
Structure deposition date
2018-01-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
38
Peptide accession
Q9UIF9
Residue number A
1720
Residue number B
1723
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1720 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1723 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1697 and 1720.

Details

Redox score ?
65
PDB code
4q6f
Structure name
crystal structure of human baz2a phd zinc finger in complex with unmodified h3k4 histone peptide
Structure deposition date
2014-04-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
14
% buried
nan
Peptide accession
Q9UIF9
Residue number A
1697
Residue number B
1720
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1697 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1720 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1701 and 1705. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
6fap
Structure name
crystal structure of human baz2a phd zinc finger in complex with fr23
Structure deposition date
2017-12-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
38
Peptide accession
Q9UIF9
Residue number A
1701
Residue number B
1705
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1701 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1705 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1682 and 1701. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
6fkp
Structure name
crystal structure of baz2a phd zinc finger in complex with h3 10-mer aa mutant peptide
Structure deposition date
2018-01-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
9
% buried
58
Peptide accession
Q9UIF9
Residue number A
1682
Residue number B
1701
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1682 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1701 of Bromodomain adjacent to zinc finger domain protein 2A

A redox-regulated disulphide may form within Bromodomain adjacent to zinc finger domain protein 2A between cysteines 1701 and 1720. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6fkp
Structure name
crystal structure of baz2a phd zinc finger in complex with h3 10-mer aa mutant peptide
Structure deposition date
2018-01-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
10
% buried
70
Peptide accession
Q9UIF9
Residue number A
1701
Residue number B
1720
Peptide name
Bromodomain adjacent to zinc finger domain protein 2A

Ligandability

Cysteine 1701 of Bromodomain adjacent to zinc finger domain protein 2A

Cysteine 1720 of Bromodomain adjacent to zinc finger domain protein 2A

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