Estrogen receptor
Intermolecular
Cysteine 530 and cysteine 417
Cysteine 227 and cysteine 227
Cysteine 221 and cysteine 221
Cysteine 237 and cysteine 237
Intramolecular
Cysteine 185 and cysteine 205
Cysteine 221 and cysteine 227
Cysteine 185 and cysteine 188
Cysteine 227 and cysteine 240
Cysteine 221 and cysteine 237
Cysteine 221 and cysteine 240
More...Cysteine 227 and cysteine 237
Cysteine 237 and cysteine 240
Cysteine 188 and cysteine 202
Cysteine 188 and cysteine 205
Cysteine 205 and cysteine 245
Cysteine 185 and cysteine 245
Cysteine 202 and cysteine 205
Cysteine 185 and cysteine 202
Cysteine 202 and cysteine 245
Cysteine 188 and cysteine 245
Cysteine 240 and cysteine 245
3os8 A 530 D 417
A redox-regulated disulphide may form between two units of Estrogen receptor at cysteines 530 and 417.
Details
Redox score ?
69
PDB code
3os8
Structure name
estrogen receptor
Structure deposition date
2010-09-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
10
Peptide A name
Estrogen receptor
Peptide B name
Estrogen receptor
Peptide A accession
P03372
Peptide B accession
P03372
Peptide A residue number
530
Peptide B residue number
417
Ligandability
Cysteine 530 of Estrogen receptor
Cysteine 417 of Estrogen receptor
1hcq E 49 F 49
A redox-regulated disulphide may form between two units of Estrogen receptor at cysteines 227 and 227 (49 and 49 respectively in this structure).
Details
Redox score ?
60
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
12
% buried
34
Peptide A name
Estrogen receptor
Peptide B name
Estrogen receptor
Peptide A accession
P03372
Peptide B accession
P03372
Peptide A residue number
227
Peptide B residue number
227
Ligandability
4aa6 E 221 F 221
A redox-regulated disulphide may form between two units of Estrogen receptor at cysteines 221 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
4aa6
Structure name
the oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
Structure deposition date
2011-11-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
24
Peptide A name
Estrogen receptor
Peptide B name
Estrogen receptor
Peptide A accession
P03372
Peptide B accession
P03372
Peptide A residue number
221
Peptide B residue number
221
Ligandability
4aa6 E 237 F 237
A redox-regulated disulphide may form between two units of Estrogen receptor at cysteines 237 and 237. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
4aa6
Structure name
the oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
Structure deposition date
2011-11-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
55
Peptide A name
Estrogen receptor
Peptide B name
Estrogen receptor
Peptide A accession
P03372
Peptide B accession
P03372
Peptide A residue number
237
Peptide B residue number
237
Ligandability
1hcq E 7 E 27
A redox-regulated disulphide may form within Estrogen receptor between cysteines 185 and 205 (7 and 27 respectively in this structure).
Details
Redox score ?
86
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
79
Minimum pKa ?
5
% buried
nan
Peptide accession
P03372
Residue number A
185
Residue number B
205
Peptide name
Estrogen receptor
Ligandability
Cysteine 185 of Estrogen receptor
Cysteine 205 of Estrogen receptor
1hcq B 43 B 49
A redox-regulated disulphide may form within Estrogen receptor between cysteines 221 and 227 (43 and 49 respectively in this structure).
Details
Redox score ?
86
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
6
% buried
37
Peptide accession
P03372
Residue number A
221
Residue number B
227
Peptide name
Estrogen receptor
Ligandability
Cysteine 221 of Estrogen receptor
Cysteine 227 of Estrogen receptor
4aa6 B 185 B 188
A redox-regulated disulphide may form within Estrogen receptor between cysteines 185 and 188.
Details
Redox score ?
84
PDB code
4aa6
Structure name
the oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
Structure deposition date
2011-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
4
% buried
68
Peptide accession
P03372
Residue number A
185
Residue number B
188
Peptide name
Estrogen receptor
Ligandability
Cysteine 185 of Estrogen receptor
Cysteine 188 of Estrogen receptor
1hcq E 49 E 62
A redox-regulated disulphide may form within Estrogen receptor between cysteines 227 and 240 (49 and 62 respectively in this structure).
Details
Redox score ?
82
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
33
Peptide accession
P03372
Residue number A
227
Residue number B
240
Peptide name
Estrogen receptor
Ligandability
Cysteine 227 of Estrogen receptor
Cysteine 240 of Estrogen receptor
1hcq B 43 B 59
A redox-regulated disulphide may form within Estrogen receptor between cysteines 221 and 237 (43 and 59 respectively in this structure).
Details
Redox score ?
81
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
6
% buried
49
Peptide accession
P03372
Residue number A
221
Residue number B
237
Peptide name
Estrogen receptor
Ligandability
Cysteine 221 of Estrogen receptor
Cysteine 237 of Estrogen receptor
1hcq A 43 A 62
A redox-regulated disulphide may form within Estrogen receptor between cysteines 221 and 240 (43 and 62 respectively in this structure).
Details
Redox score ?
79
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
6
% buried
33
Peptide accession
P03372
Residue number A
221
Residue number B
240
Peptide name
Estrogen receptor
Ligandability
Cysteine 221 of Estrogen receptor
Cysteine 240 of Estrogen receptor
1hcq F 49 F 59
A redox-regulated disulphide may form within Estrogen receptor between cysteines 227 and 237 (49 and 59 respectively in this structure).
Details
Redox score ?
73
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
42
Peptide accession
P03372
Residue number A
227
Residue number B
237
Peptide name
Estrogen receptor
Ligandability
Cysteine 227 of Estrogen receptor
Cysteine 237 of Estrogen receptor
4aa6 A 237 A 240
A redox-regulated disulphide may form within Estrogen receptor between cysteines 237 and 240.
Details
Redox score ?
71
PDB code
4aa6
Structure name
the oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
Structure deposition date
2011-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
52
Peptide accession
P03372
Residue number A
237
Residue number B
240
Peptide name
Estrogen receptor
Ligandability
Cysteine 237 of Estrogen receptor
Cysteine 240 of Estrogen receptor
1hcq E 10 E 24
A redox-regulated disulphide may form within Estrogen receptor between cysteines 188 and 202 (10 and 24 respectively in this structure).
Details
Redox score ?
63
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
14
% buried
80
Peptide accession
P03372
Residue number A
188
Residue number B
202
Peptide name
Estrogen receptor
Ligandability
Cysteine 188 of Estrogen receptor
Cysteine 202 of Estrogen receptor
4aa6 A 188 A 205
A redox-regulated disulphide may form within Estrogen receptor between cysteines 188 and 205.
Details
Redox score ?
62
PDB code
4aa6
Structure name
the oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
Structure deposition date
2011-11-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
84
Peptide accession
P03372
Residue number A
188
Residue number B
205
Peptide name
Estrogen receptor
Ligandability
Cysteine 188 of Estrogen receptor
Cysteine 205 of Estrogen receptor
4aa6 E 205 E 245
A redox-regulated disulphide may form within Estrogen receptor between cysteines 205 and 245.
Details
Redox score ?
61
PDB code
4aa6
Structure name
the oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
Structure deposition date
2011-11-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
80
Peptide accession
P03372
Residue number A
205
Residue number B
245
Peptide name
Estrogen receptor
Ligandability
Cysteine 205 of Estrogen receptor
Cysteine 245 of Estrogen receptor
4aa6 F 185 F 245
A redox-regulated disulphide may form within Estrogen receptor between cysteines 185 and 245. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
4aa6
Structure name
the oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
Structure deposition date
2011-11-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
nan
Peptide accession
P03372
Residue number A
185
Residue number B
245
Peptide name
Estrogen receptor
Ligandability
Cysteine 185 of Estrogen receptor
Cysteine 245 of Estrogen receptor
1hcq B 24 B 27
A redox-regulated disulphide may form within Estrogen receptor between cysteines 202 and 205 (24 and 27 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
72
Minimum pKa ?
22
% buried
nan
Peptide accession
P03372
Residue number A
202
Residue number B
205
Peptide name
Estrogen receptor
Ligandability
Cysteine 202 of Estrogen receptor
Cysteine 205 of Estrogen receptor
1hcq A 7 A 24
A redox-regulated disulphide may form within Estrogen receptor between cysteines 185 and 202 (7 and 24 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
23
% buried
nan
Peptide accession
P03372
Residue number A
185
Residue number B
202
Peptide name
Estrogen receptor
Ligandability
Cysteine 185 of Estrogen receptor
Cysteine 202 of Estrogen receptor
4aa6 B 202 B 245
A redox-regulated disulphide may form within Estrogen receptor between cysteines 202 and 245. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4aa6
Structure name
the oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation
Structure deposition date
2011-11-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
87
Peptide accession
P03372
Residue number A
202
Residue number B
245
Peptide name
Estrogen receptor
Ligandability
Cysteine 202 of Estrogen receptor
Cysteine 245 of Estrogen receptor
1hcq A 10 A 67
A redox-regulated disulphide may form within Estrogen receptor between cysteines 188 and 245 (10 and 67 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
1hcq
Structure name
the crystal structure of the estrogen receptor dna-binding domain bound to dna: how receptors discriminate between their response elements
Structure deposition date
1995-01-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
76
Peptide accession
P03372
Residue number A
188
Residue number B
245
Peptide name
Estrogen receptor
Ligandability
Cysteine 188 of Estrogen receptor
Cysteine 245 of Estrogen receptor
1hcp A 62 A 67
A redox-regulated disulphide may form within Estrogen receptor between cysteines 240 and 245 (62 and 67 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
1hcp
Structure name
dna recognition by the oestrogen receptor: from solution to the crystal
Structure deposition date
1993-11-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
9
% buried
36
Peptide accession
P03372
Residue number A
240
Residue number B
245
Peptide name
Estrogen receptor
Ligandability
Cysteine 240 of Estrogen receptor
Cysteine 245 of Estrogen receptor
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