Bromodomain-containing protein 1
Intramolecular
Cysteine 217 and cysteine 245
Cysteine 217 and cysteine 220
Cysteine 234 and cysteine 261
Cysteine 234 and cysteine 237
Cysteine 258 and cysteine 261
Cysteine 341 and cysteine 346
Cysteine 237 and cysteine 261
Cysteine 327 and cysteine 354
Cysteine 327 and cysteine 330
Cysteine 234 and cysteine 258
More...Cysteine 237 and cysteine 258
Cysteine 220 and cysteine 245
Cysteine 341 and cysteine 385
Cysteine 346 and cysteine 385
Cysteine 330 and cysteine 354
2l43 A 28 A 56
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 217 and 245 (28 and 56 respectively in this structure).
Details
Redox score ?
89
PDB code
2l43
Structure name
structural basis for histone code recognition by brpf2-phd1 finger
Structure deposition date
2010-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
4
Peptide accession
O95696
Residue number A
217
Residue number B
245
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 217 of Bromodomain-containing protein 1
Cysteine 245 of Bromodomain-containing protein 1
2ku3 A 10 A 13
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 217 and 220 (10 and 13 respectively in this structure).
Details
Redox score ?
89
PDB code
2ku3
Structure name
solution structure of brd1 phd1 finger
Structure deposition date
2010-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
2
Peptide accession
O95696
Residue number A
217
Residue number B
220
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 217 of Bromodomain-containing protein 1
Cysteine 220 of Bromodomain-containing protein 1
2ku3 A 27 A 54
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 234 and 261 (27 and 54 respectively in this structure).
Details
Redox score ?
87
PDB code
2ku3
Structure name
solution structure of brd1 phd1 finger
Structure deposition date
2010-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
7
Peptide accession
O95696
Residue number A
234
Residue number B
261
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 234 of Bromodomain-containing protein 1
Cysteine 261 of Bromodomain-containing protein 1
2l43 A 45 A 48
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 234 and 237 (45 and 48 respectively in this structure).
Details
Redox score ?
86
PDB code
2l43
Structure name
structural basis for histone code recognition by brpf2-phd1 finger
Structure deposition date
2010-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
3
Peptide accession
O95696
Residue number A
234
Residue number B
237
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 234 of Bromodomain-containing protein 1
Cysteine 237 of Bromodomain-containing protein 1
2l43 A 69 A 72
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 258 and 261 (69 and 72 respectively in this structure).
Details
Redox score ?
85
PDB code
2l43
Structure name
structural basis for histone code recognition by brpf2-phd1 finger
Structure deposition date
2010-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
7
% buried
0
Peptide accession
O95696
Residue number A
258
Residue number B
261
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 258 of Bromodomain-containing protein 1
Cysteine 261 of Bromodomain-containing protein 1
2lq6 A 341 A 346
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 341 and 346.
Details
Redox score ?
85
PDB code
2lq6
Structure name
solution structure of brd1 phd2 finger
Structure deposition date
2012-02-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
8
Peptide accession
O95696
Residue number A
341
Residue number B
346
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 341 of Bromodomain-containing protein 1
Cysteine 346 of Bromodomain-containing protein 1
2ku3 A 30 A 54
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 237 and 261 (30 and 54 respectively in this structure).
Details
Redox score ?
85
PDB code
2ku3
Structure name
solution structure of brd1 phd1 finger
Structure deposition date
2010-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
6
% buried
0
Peptide accession
O95696
Residue number A
237
Residue number B
261
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 237 of Bromodomain-containing protein 1
Cysteine 261 of Bromodomain-containing protein 1
2lq6 A 327 A 354
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 327 and 354.
Details
Redox score ?
84
PDB code
2lq6
Structure name
solution structure of brd1 phd2 finger
Structure deposition date
2012-02-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
2
Peptide accession
O95696
Residue number A
327
Residue number B
354
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 327 of Bromodomain-containing protein 1
Cysteine 354 of Bromodomain-containing protein 1
2lq6 A 327 A 330
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 327 and 330.
Details
Redox score ?
83
PDB code
2lq6
Structure name
solution structure of brd1 phd2 finger
Structure deposition date
2012-02-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
2
Peptide accession
O95696
Residue number A
327
Residue number B
330
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 327 of Bromodomain-containing protein 1
Cysteine 330 of Bromodomain-containing protein 1
2ku3 A 27 A 51
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 234 and 258 (27 and 51 respectively in this structure).
Details
Redox score ?
83
PDB code
2ku3
Structure name
solution structure of brd1 phd1 finger
Structure deposition date
2010-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
7
% buried
7
Peptide accession
O95696
Residue number A
234
Residue number B
258
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 234 of Bromodomain-containing protein 1
Cysteine 258 of Bromodomain-containing protein 1
2ku3 A 30 A 51
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 237 and 258 (30 and 51 respectively in this structure).
Details
Redox score ?
82
PDB code
2ku3
Structure name
solution structure of brd1 phd1 finger
Structure deposition date
2010-02-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
0
Peptide accession
O95696
Residue number A
237
Residue number B
258
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 237 of Bromodomain-containing protein 1
Cysteine 258 of Bromodomain-containing protein 1
2l43 A 31 A 56
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 220 and 245 (31 and 56 respectively in this structure).
Details
Redox score ?
82
PDB code
2l43
Structure name
structural basis for histone code recognition by brpf2-phd1 finger
Structure deposition date
2010-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
O95696
Residue number A
220
Residue number B
245
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 220 of Bromodomain-containing protein 1
Cysteine 245 of Bromodomain-containing protein 1
2lq6 A 341 A 385
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 341 and 385.
Details
Redox score ?
80
PDB code
2lq6
Structure name
solution structure of brd1 phd2 finger
Structure deposition date
2012-02-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
8
% buried
16
Peptide accession
O95696
Residue number A
341
Residue number B
385
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 341 of Bromodomain-containing protein 1
Cysteine 385 of Bromodomain-containing protein 1
2lq6 A 346 A 385
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 346 and 385.
Details
Redox score ?
79
PDB code
2lq6
Structure name
solution structure of brd1 phd2 finger
Structure deposition date
2012-02-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
8
Peptide accession
O95696
Residue number A
346
Residue number B
385
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 346 of Bromodomain-containing protein 1
Cysteine 385 of Bromodomain-containing protein 1
2lq6 A 330 A 354
A redox-regulated disulphide may form within Bromodomain-containing protein 1 between cysteines 330 and 354.
Details
Redox score ?
79
PDB code
2lq6
Structure name
solution structure of brd1 phd2 finger
Structure deposition date
2012-02-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
8
% buried
0
Peptide accession
O95696
Residue number A
330
Residue number B
354
Peptide name
Bromodomain-containing protein 1
Ligandability
Cysteine 330 of Bromodomain-containing protein 1
Cysteine 354 of Bromodomain-containing protein 1
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