ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Ankyrin-2

Intramolecular
Cysteine 1348 and cysteine 1446
Cysteine 1346 and cysteine 1385
Cysteine 1346 and cysteine 1446
A redox-regulated disulphide may form within Ankyrin-2 between cysteines 1348 and 1446. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6m3q
Structure name
crystal structure of ankb/beta4-spectrin complex
Structure deposition date
2020-03-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
80
Peptide accession
Q01484
Residue number A
1348
Residue number B
1446
Peptide name
Ankyrin-2

Ligandability

Cysteine 1348 of Ankyrin-2

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 1446 of Ankyrin-2

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 Ankyrin-2 between cysteines 1346 and 1385 (1313 and 1352 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
4d8o
Structure name
crystal structure of the ankyrin-b zu5-zu5-upa-dd tandem
Structure deposition date
2012-01-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
80
Peptide accession
Q01484
Residue number A
1346
Residue number B
1385
Peptide name
Ankyrin-2

Ligandability

Cysteine 1346 of Ankyrin-2

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 1385 of Ankyrin-2

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 Ankyrin-2 between cysteines 1346 and 1446 (1313 and 1413 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4d8o
Structure name
crystal structure of the ankyrin-b zu5-zu5-upa-dd tandem
Structure deposition date
2012-01-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
80
Peptide accession
Q01484
Residue number A
1346
Residue number B
1446
Peptide name
Ankyrin-2

Ligandability

Cysteine 1346 of Ankyrin-2

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 1446 of Ankyrin-2

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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