ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Retinoic acid receptor gamma

Intramolecular
Cysteine 237 and cysteine 267
Cysteine 335 and cysteine 338
Cysteine 267 and cysteine 335
A redox-regulated disulphide may form within Retinoic acid receptor gamma between cysteines 237 and 267. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
1fcy
Structure name
isotype selectivity of the human retinoic acid nuclear receptor hrar: the complex with the rarbeta/gamma-selective retinoid cd564
Structure deposition date
2000-07-19
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
100
Peptide accession
P13631
Residue number A
237
Residue number B
267
Peptide name
Retinoic acid receptor gamma

Ligandability

Cysteine 237 of Retinoic acid receptor gamma

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 267 of Retinoic acid receptor gamma

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 gamma between cysteines 335 and 338. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1fcx
Structure name
isotype selectivity of the human retinoic acid nuclear receptor hrar: the complex with the rargamma-selective retinoid bms184394
Structure deposition date
2000-07-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
10
% buried
80
Peptide accession
P13631
Residue number A
335
Residue number B
338
Peptide name
Retinoic acid receptor gamma

Ligandability

Cysteine 335 of Retinoic acid receptor gamma

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 338 of Retinoic acid receptor gamma

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 gamma between cysteines 267 and 335. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
1fcz
Structure name
isotype selectivity of the human retinoic acid nuclear receptor hrar: the complex with the panagonist retinoid bms181156
Structure deposition date
2000-07-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
P13631
Residue number A
267
Residue number B
335
Peptide name
Retinoic acid receptor gamma

Ligandability

Cysteine 267 of Retinoic acid receptor gamma

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 335 of Retinoic acid receptor gamma

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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