ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Endothelial PAS domain-containing protein 1

Intermolecular
Cysteine 542 and cysteine 77 of von Hippel-Lindau disease tumor suppressor L
Intramolecular
Cysteine 195 and cysteine 226
Cysteine 297 and cysteine 339
Cysteine 336 and cysteine 339
Cysteine 257 and cysteine 339
A redox-regulated disulphide may form between cysteine 542 of Endothelial PAS domain-containing protein 1 and cysteine 77 of von Hippel-Lindau disease tumor suppressor.

Details

Redox score ?
86
PDB code
6i7q
Structure name
structure of pvhl-elongin b-elongin c (vcb) in complex with hydroxylated-hif-2alpha (523-542) in the c2221 form
Structure deposition date
2018-11-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide A name
Endothelial PAS domain-containing protein 1
Peptide B name
von Hippel-Lindau disease tumor suppressor
Peptide A accession
Q99814
Peptide B accession
P40337
Peptide A residue number
542
Peptide B residue number
77

Ligandability

Cysteine 542 of Endothelial PAS domain-containing protein 1

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 77 of von Hippel-Lindau disease tumor suppressor

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 542 in protein A could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within Endothelial PAS domain-containing protein 1 between cysteines 195 and 226.

Details

Redox score ?
71
PDB code
6e3u
Structure name
crystal structure of the heterodimeric hif-2 complex with agonist m1001
Structure deposition date
2018-07-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
77
Minimum pKa ?
9
% buried
100
Peptide accession
P97481
Residue number A
195
Residue number B
226
Peptide name
Endothelial PAS domain-containing protein 1

Ligandability

Cysteine 195 of Endothelial PAS domain-containing protein 1

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 226 of Endothelial PAS domain-containing protein 1

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 Endothelial PAS domain-containing protein 1 between cysteines 297 and 339 (61 and 103 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
2a24
Structure name
haddock structure of hif-2a/arnt pas-b heterodimer
Structure deposition date
2005-06-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
59
Peptide accession
Q99814
Residue number A
297
Residue number B
339
Peptide name
Endothelial PAS domain-containing protein 1

Ligandability

Cysteine 297 of Endothelial PAS domain-containing protein 1

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 339 of Endothelial PAS domain-containing protein 1

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 Endothelial PAS domain-containing protein 1 between cysteines 336 and 339. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
7w80
Structure name
crystal structure of the heterodimeric hif-2 in complex with antagonist belzutifan
Structure deposition date
2021-12-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
72
Peptide accession
P97481
Residue number A
336
Residue number B
339
Peptide name
Endothelial PAS domain-containing protein 1

Ligandability

Cysteine 336 of Endothelial PAS domain-containing protein 1

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 339 of Endothelial PAS domain-containing protein 1

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 Endothelial PAS domain-containing protein 1 between cysteines 257 and 339. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
6d0c
Structure name
crystal structure of hif2a-b*:arnt-b* complex
Structure deposition date
2018-04-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
80
Peptide accession
Q99814
Residue number A
257
Residue number B
339
Peptide name
Endothelial PAS domain-containing protein 1

Ligandability

Cysteine 257 of Endothelial PAS domain-containing protein 1

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 339 of Endothelial PAS domain-containing protein 1

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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