ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Nuclear receptor ROR-alpha

Intramolecular
Cysteine 369 and cysteine 411
Cysteine 323 and cysteine 396
Cysteine 288 and cysteine 369
A redox-regulated disulphide may form within Nuclear receptor ROR-alpha between cysteines 369 and 411. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
4s15
Structure name
crystal structure of the orphan nuclear receptor roralpha ligand- binding domain in complex with 4alpha-caboxyl, 4beta-methyl- zymosterol (4acd8)
Structure deposition date
2015-01-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
83
Peptide accession
P35398
Residue number A
369
Residue number B
411
Peptide name
Nuclear receptor ROR-alpha

Ligandability

Cysteine 369 of Nuclear receptor ROR-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 411 of Nuclear receptor ROR-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 Nuclear receptor ROR-alpha between cysteines 323 and 396. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4s15
Structure name
crystal structure of the orphan nuclear receptor roralpha ligand- binding domain in complex with 4alpha-caboxyl, 4beta-methyl- zymosterol (4acd8)
Structure deposition date
2015-01-08
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
78
Peptide accession
P35398
Residue number A
323
Residue number B
396
Peptide name
Nuclear receptor ROR-alpha

Ligandability

Cysteine 323 of Nuclear receptor ROR-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 396 of Nuclear receptor ROR-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 Nuclear receptor ROR-alpha between cysteines 288 and 369. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
1s0x
Structure name
crystal structure of the human roralpha ligand binding domain in complex with cholesterol sulfate at 2
Structure deposition date
2004-01-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
7
% buried
92
Peptide accession
P35398
Residue number A
288
Residue number B
369
Peptide name
Nuclear receptor ROR-alpha

Ligandability

Cysteine 288 of Nuclear receptor ROR-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 369 of Nuclear receptor ROR-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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