ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Retinoic acid receptor RXR-alpha

Intermolecular
Cysteine 269 and cysteine 269
Intramolecular
Cysteine 171 and cysteine 177
Cysteine 177 and cysteine 187
Cysteine 171 and cysteine 187
Cysteine 135 and cysteine 138 L
Cysteine 138 and cysteine 155 L
Cysteine 135 and cysteine 152 L
Cysteine 187 and cysteine 190
Cysteine 171 and cysteine 190
Cysteine 177 and cysteine 190
More...
Cysteine 135 and cysteine 155 L
Cysteine 138 and cysteine 152 L
Cysteine 135 and cysteine 195 L
Cysteine 152 and cysteine 155
Cysteine 155 and cysteine 195
Cysteine 152 and cysteine 195
Cysteine 138 and cysteine 195 L
Cysteine 138 and cysteine 187 L
Cysteine 274 and cysteine 437
Cysteine 374 and cysteine 409
A redox-regulated disulphide may form between two units of Retinoic acid receptor RXR-alpha at cysteines 269 and 269.

Details

Redox score ?
83
PDB code
4n8r
Structure name
crystal structure of rxra lbd complexed with a synthetic modulator k- 8008
Structure deposition date
2013-10-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide A name
Retinoic acid receptor RXR-alpha
Peptide B name
Retinoic acid receptor RXR-alpha
Peptide A accession
P19793
Peptide B accession
P19793
Peptide A residue number
269
Peptide B residue number
269

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 171 and 177 (1271 and 1277 respectively in this structure).

Details

Redox score ?
88
PDB code
1by4
Structure name
structure and mechanism of the homodimeric assembly of the rxr on dna
Structure deposition date
1998-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
8
Peptide accession
P19793
Residue number A
171
Residue number B
177
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 171 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 177 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 177 and 187 (2177 and 2187 respectively in this structure).

Details

Redox score ?
87
PDB code
1by4
Structure name
structure and mechanism of the homodimeric assembly of the rxr on dna
Structure deposition date
1998-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
10
Peptide accession
P19793
Residue number A
177
Residue number B
187
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 177 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 187 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 171 and 187.

Details

Redox score ?
85
PDB code
4nqa
Structure name
crystal structure of liganded hrxr-alpha/hlxr-beta heterodimer on dna
Structure deposition date
2013-11-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
44
Peptide accession
P19793
Residue number A
171
Residue number B
187
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 171 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 187 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 135 and 138 (1235 and 1238 respectively in this structure).

Details

Redox score ?
84
PDB code
1dsz
Structure name
structure of the rxr/rar dna-binding domain heterodimer in complex with the retinoic acid response element dr1
Structure deposition date
2000-01-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
4
% buried
nan
Peptide accession
P19793
Residue number A
135
Residue number B
138
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 135 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 138 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 138 and 155.

Details

Redox score ?
82
PDB code
3dzu
Structure name
intact ppar gamma - rxr alpha nuclear receptor complex on dna bound with bvt
Structure deposition date
2008-07-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
5
% buried
72
Peptide accession
P19793
Residue number A
138
Residue number B
155
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 138 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 155 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 135 and 152 (2235 and 2252 respectively in this structure).

Details

Redox score ?
81
PDB code
1by4
Structure name
structure and mechanism of the homodimeric assembly of the rxr on dna
Structure deposition date
1998-10-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
5
% buried
83
Peptide accession
P19793
Residue number A
135
Residue number B
152
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 135 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 152 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 187 and 190.

Details

Redox score ?
80
PDB code
3e00
Structure name
intact ppar gamma - rxr alpha nuclear receptor complex on dna bound with gw9662, 9-cis retinoic acid and ncoa2 peptide
Structure deposition date
2008-07-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
30
Peptide accession
P19793
Residue number A
187
Residue number B
190
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 187 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 190 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 171 and 190.

Details

Redox score ?
79
PDB code
4cn3
Structure name
crystal structure of the human retinoid x receptor dna- binding domain bound to the human gde1spa response element
Structure deposition date
2014-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
32
Peptide accession
P19793
Residue number A
171
Residue number B
190
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 171 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 190 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 177 and 190.

Details

Redox score ?
78
PDB code
2nll
Structure name
retinoid x receptor-thyroid hormone receptor dna-binding domain heterodimer bound to thyroid response element dna
Structure deposition date
1996-11-20
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
8
Peptide accession
P19793
Residue number A
177
Residue number B
190
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 177 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 190 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 135 and 155.

Details

Redox score ?
67
PDB code
4cn2
Structure name
crystal structure of the human retinoid x receptor dna- binding domain bound to the human ramp2 response element
Structure deposition date
2014-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
86
Peptide accession
P19793
Residue number A
135
Residue number B
155
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 135 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 155 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 138 and 152.

Details

Redox score ?
65
PDB code
4cn7
Structure name
crystal structure of the human retinoid x receptor dna- binding domain bound to an idealized dr1 response element
Structure deposition date
2014-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
13
% buried
73
Peptide accession
P19793
Residue number A
138
Residue number B
152
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 138 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 152 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 135 and 195.

Details

Redox score ?
65
PDB code
4cn3
Structure name
crystal structure of the human retinoid x receptor dna- binding domain bound to the human gde1spa response element
Structure deposition date
2014-01-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
5
% buried
80
Peptide accession
P19793
Residue number A
135
Residue number B
195
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 135 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 195 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 152 and 155.

Details

Redox score ?
64
PDB code
4cn7
Structure name
crystal structure of the human retinoid x receptor dna- binding domain bound to an idealized dr1 response element
Structure deposition date
2014-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
14
% buried
nan
Peptide accession
P19793
Residue number A
152
Residue number B
155
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 152 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 155 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 155 and 195 (121 and 161 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
1r0n
Structure name
crystal structure of heterodimeric ecdsyone receptor dna binding complex
Structure deposition date
2003-09-22
Thiol separation (Å)
5
Half-sphere exposure sum ?
79
Minimum pKa ?
16
% buried
nan
Peptide accession
P19793
Residue number A
155
Residue number B
195
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 155 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 195 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 152 and 195. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3dzy
Structure name
intact ppar gamma - rxr alpha nuclear receptor complex on dna bound with rosiglitazone, 9-cis retinoic acid and ncoa2 peptide
Structure deposition date
2008-07-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
4
% buried
88
Peptide accession
P19793
Residue number A
152
Residue number B
195
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 152 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 195 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 138 and 195. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
4cn3
Structure name
crystal structure of the human retinoid x receptor dna- binding domain bound to the human gde1spa response element
Structure deposition date
2014-01-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
5
% buried
75
Peptide accession
P19793
Residue number A
138
Residue number B
195
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 138 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 195 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 138 and 187. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1rxr
Structure name
high resolution solution structure of the retinoid x receptor dna binding domain, nmr, 20 structure
Structure deposition date
1998-06-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
29
Peptide accession
P19793
Residue number A
138
Residue number B
187
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 138 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Ligandable in the dataset of Kuljanin et al.

Cysteine 187 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 274 and 437. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
3a9e
Structure name
crystal structure of a mixed agonist-bound rar-alpha and antagonist- bound rxr-alpha heterodimer ligand binding domains
Structure deposition date
2009-10-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
62
Peptide accession
P28700
Residue number A
274
Residue number B
437
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 274 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 437 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Retinoic acid receptor RXR-alpha between cysteines 374 and 409 (369 and 404 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7aos
Structure name
crystal structure of the raralpha/rxralpha ligand binding domain heterodimer in complex with a fragment of src1 coactivator
Structure deposition date
2020-10-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
90
Peptide accession
P28700
Residue number A
374
Residue number B
409
Peptide name
Retinoic acid receptor RXR-alpha

Ligandability

Cysteine 374 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 409 of Retinoic acid receptor RXR-alpha

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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