ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Potassium-transporting ATPase alpha chain 2

Intramolecular
Cysteine 223 and cysteine 261
Cysteine 386 and cysteine 717
Cysteine 530 and cysteine 596
Cysteine 530 and cysteine 568
Cysteine 440 and cysteine 568
Cysteine 568 and cysteine 596
A redox-regulated disulphide may form within Potassium-transporting ATPase alpha chain 2 between cysteines 223 and 261.

Details

Redox score ?
78
PDB code
7x20
Structure name
crystal structure of non gastric h,k-atpase alpha2 in (k+)e2-alf state
Structure deposition date
2022-02-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
50
Peptide accession
P54708
Residue number A
223
Residue number B
261
Peptide name
Potassium-transporting ATPase alpha chain 2

Ligandability

Cysteine 223 of Potassium-transporting ATPase alpha chain 2

Cysteine 261 of Potassium-transporting ATPase alpha chain 2

A redox-regulated disulphide may form within Potassium-transporting ATPase alpha chain 2 between cysteines 386 and 717.

Details

Redox score ?
69
PDB code
7x20
Structure name
crystal structure of non gastric h,k-atpase alpha2 in (k+)e2-alf state
Structure deposition date
2022-02-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
8
% buried
98
Peptide accession
P54708
Residue number A
386
Residue number B
717
Peptide name
Potassium-transporting ATPase alpha chain 2

Ligandability

Cysteine 386 of Potassium-transporting ATPase alpha chain 2

Cysteine 717 of Potassium-transporting ATPase alpha chain 2

A redox-regulated disulphide may form within Potassium-transporting ATPase alpha chain 2 between cysteines 530 and 596. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7x20
Structure name
crystal structure of non gastric h,k-atpase alpha2 in (k+)e2-alf state
Structure deposition date
2022-02-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
70
Peptide accession
P54708
Residue number A
530
Residue number B
596
Peptide name
Potassium-transporting ATPase alpha chain 2

Ligandability

Cysteine 530 of Potassium-transporting ATPase alpha chain 2

Cysteine 596 of Potassium-transporting ATPase alpha chain 2

A redox-regulated disulphide may form within Potassium-transporting ATPase alpha chain 2 between cysteines 530 and 568. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
7x20
Structure name
crystal structure of non gastric h,k-atpase alpha2 in (k+)e2-alf state
Structure deposition date
2022-02-25
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
11
% buried
82
Peptide accession
P54708
Residue number A
530
Residue number B
568
Peptide name
Potassium-transporting ATPase alpha chain 2

Ligandability

Cysteine 530 of Potassium-transporting ATPase alpha chain 2

Cysteine 568 of Potassium-transporting ATPase alpha chain 2

A redox-regulated disulphide may form within Potassium-transporting ATPase alpha chain 2 between cysteines 440 and 568. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7x20
Structure name
crystal structure of non gastric h,k-atpase alpha2 in (k+)e2-alf state
Structure deposition date
2022-02-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
92
Minimum pKa ?
11
% buried
98
Peptide accession
P54708
Residue number A
440
Residue number B
568
Peptide name
Potassium-transporting ATPase alpha chain 2

Ligandability

Cysteine 440 of Potassium-transporting ATPase alpha chain 2

Cysteine 568 of Potassium-transporting ATPase alpha chain 2

A redox-regulated disulphide may form within Potassium-transporting ATPase alpha chain 2 between cysteines 568 and 596. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
7x20
Structure name
crystal structure of non gastric h,k-atpase alpha2 in (k+)e2-alf state
Structure deposition date
2022-02-25
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
83
Peptide accession
P54708
Residue number A
568
Residue number B
596
Peptide name
Potassium-transporting ATPase alpha chain 2

Ligandability

Cysteine 568 of Potassium-transporting ATPase alpha chain 2

Cysteine 596 of Potassium-transporting ATPase alpha chain 2

If this tool was useful for finding a disulphide, please cite: