ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aryl hydrocarbon receptor nuclear translocator

Intramolecular
Cysteine 265 and cysteine 308
Cysteine 181 and cysteine 336
Cysteine 400 and cysteine 459
Cysteine 380 and cysteine 459
A redox-regulated disulphide may form within Aryl hydrocarbon receptor nuclear translocator between cysteines 265 and 308.

Details

Redox score ?
75
PDB code
7xi4
Structure name
crystal structure of the npas4-arnt heterodimer in complex with dna
Structure deposition date
2022-04-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
8
% buried
93
Peptide accession
P53762
Residue number A
265
Residue number B
308
Peptide name
Aryl hydrocarbon receptor nuclear translocator

Ligandability

Cysteine 265 of Aryl hydrocarbon receptor nuclear translocator

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 308 of Aryl hydrocarbon receptor nuclear translocator

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 Aryl hydrocarbon receptor nuclear translocator between cysteines 181 and 336. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
5v0l
Structure name
crystal structure of the ahr-arnt heterodimer in complex with the dre
Structure deposition date
2017-02-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
18
Peptide accession
P27540
Residue number A
181
Residue number B
336
Peptide name
Aryl hydrocarbon receptor nuclear translocator

Ligandability

Cysteine 181 of Aryl hydrocarbon receptor nuclear translocator

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 336 of Aryl hydrocarbon receptor nuclear translocator

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 Aryl hydrocarbon receptor nuclear translocator between cysteines 400 and 459 (49 and 108 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
1x0o
Structure name
human arnt c-terminal pas domain
Structure deposition date
2005-03-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
82
Peptide accession
P27540
Residue number A
400
Residue number B
459
Peptide name
Aryl hydrocarbon receptor nuclear translocator

Ligandability

Cysteine 400 of Aryl hydrocarbon receptor nuclear translocator

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 459 of Aryl hydrocarbon receptor nuclear translocator

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 Aryl hydrocarbon receptor nuclear translocator between cysteines 380 and 459 (29 and 108 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2a24
Structure name
haddock structure of hif-2a/arnt pas-b heterodimer
Structure deposition date
2005-06-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
77
Peptide accession
P27540
Residue number A
380
Residue number B
459
Peptide name
Aryl hydrocarbon receptor nuclear translocator

Ligandability

Cysteine 380 of Aryl hydrocarbon receptor nuclear translocator

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 459 of Aryl hydrocarbon receptor nuclear translocator

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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