ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Importin subunit alpha-5

Intramolecular
Cysteine 240 and cysteine 255 L
Cysteine 298 and cysteine 337
Cysteine 424 and cysteine 429
A redox-regulated disulphide may form within Importin subunit alpha-5 between cysteines 240 and 255.

Details

Redox score ?
68
PDB code
6wx9
Structure name
sox2 bound to importin-alpha 5
Structure deposition date
2020-05-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
99
Peptide accession
P52294
Residue number A
240
Residue number B
255
Peptide name
Importin subunit alpha-5

Ligandability

Cysteine 240 of Importin subunit alpha-5

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 255 of Importin subunit alpha-5

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 Importin subunit alpha-5 between cysteines 298 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
2jdq
Structure name
c-terminal domain of influenza a virus polymerase pb2 subunit in complex with human importin alpha5
Structure deposition date
2007-01-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
100
Peptide accession
P52294
Residue number A
298
Residue number B
337
Peptide name
Importin subunit alpha-5

Ligandability

Cysteine 298 of Importin subunit alpha-5

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 337 of Importin subunit alpha-5

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 Importin subunit alpha-5 between cysteines 424 and 429. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6wx9
Structure name
sox2 bound to importin-alpha 5
Structure deposition date
2020-05-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
87
Peptide accession
P52294
Residue number A
424
Residue number B
429
Peptide name
Importin subunit alpha-5

Ligandability

Cysteine 424 of Importin subunit alpha-5

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 429 of Importin subunit alpha-5

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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