ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Potassium-transporting ATPase alpha chain 1

Intramolecular
Cysteine 155 and cysteine 259
Cysteine 528 and cysteine 566
Cysteine 384 and cysteine 715
Cysteine 1022 and cysteine 1023
Cysteine 977 and cysteine 980
Cysteine 974 and cysteine 977
Cysteine 528 and cysteine 259
Cysteine 121 and cysteine 814
Cysteine 893 and cysteine 928
Cysteine 566 and cysteine 259
Cysteine 438 and cysteine 566
A redox-regulated disulphide may form within Potassium-transporting ATPase alpha chain 1 between cysteines 155 and 259 (220 and 258 respectively in this structure).

Details

Redox score ?
71
PDB code
7w47
Structure name
crystal structure of the gastric proton pump complexed with tegoprazan
Structure deposition date
2021-11-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19156
Residue number A
155
Residue number B
259
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 155 of Potassium-transporting ATPase alpha chain 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 259 of Potassium-transporting ATPase alpha chain 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.

Uncertain whether structure cysteine 220 has been assigned to correct residue.
A redox-regulated disulphide may form within Potassium-transporting ATPase alpha chain 1 between cysteines 528 and 566 (527 and 565 respectively in this structure).

Details

Redox score ?
68
PDB code
6jxk
Structure name
rb+-bound e2-mgf state of the gastric proton pump (wild-type)
Structure deposition date
2019-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
9
% buried
95
Peptide accession
P19156
Residue number A
528
Residue number B
566
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 528 of Potassium-transporting ATPase alpha chain 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 566 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 384 and 715 (383 and 714 respectively in this structure).

Details

Redox score ?
66
PDB code
6jxj
Structure name
rb+-bound e2-alf state of the gastric proton pump (tyr799trp)
Structure deposition date
2019-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19156
Residue number A
384
Residue number B
715
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 384 of Potassium-transporting ATPase alpha chain 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 715 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 1022 and 1023 (1021 and 1022 respectively in this structure).

Details

Redox score ?
62
PDB code
6jxj
Structure name
rb+-bound e2-alf state of the gastric proton pump (tyr799trp)
Structure deposition date
2019-04-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
34
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19156
Residue number A
1022
Residue number B
1023
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 1022 of Potassium-transporting ATPase alpha chain 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 1023 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 977 and 980 (976 and 979 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
6jxk
Structure name
rb+-bound e2-mgf state of the gastric proton pump (wild-type)
Structure deposition date
2019-04-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
58
Peptide accession
P19156
Residue number A
977
Residue number B
980
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 977 of Potassium-transporting ATPase alpha chain 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 980 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 974 and 977 (973 and 976 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
7w48
Structure name
crystal structure of the gastric proton pump complexed with pf- 03716556
Structure deposition date
2021-11-26
Thiol separation (Å)
6
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19156
Residue number A
974
Residue number B
977
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 974 of Potassium-transporting ATPase alpha chain 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 977 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 528 and 259 (527 and 593 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6jxi
Structure name
rb+-bound e2-mgf state of the gastric proton pump (tyr799trp)
Structure deposition date
2019-04-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19156
Residue number A
528
Residue number B
259
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 528 of Potassium-transporting ATPase alpha chain 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 259 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 121 and 814 (120 and 813 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
7w47
Structure name
crystal structure of the gastric proton pump complexed with tegoprazan
Structure deposition date
2021-11-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19156
Residue number A
121
Residue number B
814
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 121 of Potassium-transporting ATPase alpha chain 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 814 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 893 and 928 (892 and 927 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7w49
Structure name
crystal structure of the gastric proton pump complexed with soraprazan
Structure deposition date
2021-11-26
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19156
Residue number A
893
Residue number B
928
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 893 of Potassium-transporting ATPase alpha chain 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 928 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 566 and 259 (565 and 593 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
7w49
Structure name
crystal structure of the gastric proton pump complexed with soraprazan
Structure deposition date
2021-11-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P19156
Residue number A
566
Residue number B
259
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 566 of Potassium-transporting ATPase alpha chain 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 259 of Potassium-transporting ATPase alpha chain 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 Potassium-transporting ATPase alpha chain 1 between cysteines 438 and 566 (437 and 565 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6jxk
Structure name
rb+-bound e2-mgf state of the gastric proton pump (wild-type)
Structure deposition date
2019-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
9
% buried
100
Peptide accession
P19156
Residue number A
438
Residue number B
566
Peptide name
Potassium-transporting ATPase alpha chain 1

Ligandability

Cysteine 438 of Potassium-transporting ATPase alpha chain 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 566 of Potassium-transporting ATPase alpha chain 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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