ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein 4.2

Intramolecular
Cysteine 398 and cysteine 399
Cysteine 173 and cysteine 586
Cysteine 621 and cysteine 670
Cysteine 332 and cysteine 363
Cysteine 276 and cysteine 332
A redox-regulated disulphide may form within Protein 4.2 between cysteines 398 and 399. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7tw5
Structure name
cryo-em structure of human ankyrin complex (b2p1a2) from red blood cell
Structure deposition date
2022-02-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
12
Peptide accession
P16452
Residue number A
398
Residue number B
399
Peptide name
Protein 4

Ligandability

Cysteine 398 of Protein 4.2

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 399 of Protein 4.2

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 Protein 4.2 between cysteines 173 and 586. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
7tw5
Structure name
cryo-em structure of human ankyrin complex (b2p1a2) from red blood cell
Structure deposition date
2022-02-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
28
Peptide accession
P16452
Residue number A
173
Residue number B
586
Peptide name
Protein 4

Ligandability

Cysteine 173 of Protein 4.2

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 586 of Protein 4.2

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 Protein 4.2 between cysteines 621 and 670. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7tw1
Structure name
cryo-em structure of human band 3-protein 4
Structure deposition date
2022-02-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
11
% buried
70
Peptide accession
P16452
Residue number A
621
Residue number B
670
Peptide name
Protein 4

Ligandability

Cysteine 621 of Protein 4.2

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 670 of Protein 4.2

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 Protein 4.2 between cysteines 332 and 363. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7v0q
Structure name
local refinement of protein 4
Structure deposition date
2022-05-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
92
Peptide accession
P16452
Residue number A
332
Residue number B
363
Peptide name
Protein 4

Ligandability

Cysteine 332 of Protein 4.2

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 363 of Protein 4.2

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 Protein 4.2 between cysteines 276 and 332. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
7tvz
Structure name
cryo-em structure of human band 3-protein 4
Structure deposition date
2022-02-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
100
Peptide accession
P16452
Residue number A
276
Residue number B
332
Peptide name
Protein 4

Ligandability

Cysteine 276 of Protein 4.2

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 332 of Protein 4.2

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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