ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Polyamine-transporting ATPase 13A2

Intramolecular
Cysteine 41 and cysteine 80
Cysteine 298 and cysteine 317
Cysteine 871 and cysteine 910
Cysteine 1136 and cysteine 1140
Cysteine 291 and cysteine 293
Cysteine 189 and cysteine 360 L
Cysteine 324 and cysteine 371
Cysteine 475 and cysteine 920
Cysteine 296 and cysteine 317
Cysteine 329 and cysteine 401
More...
Cysteine 376 and cysteine 401
Cysteine 317 and cysteine 329
A redox-regulated disulphide may form within Polyamine-transporting ATPase 13A2 between cysteines 41 and 80.

Details

Redox score ?
78
PDB code
7vpk
Structure name
cryo-em structure of the human atp13a2 (spm-bound e2p state)
Structure deposition date
2021-10-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
8
% buried
0
Peptide accession
Q9NQ11
Residue number A
41
Residue number B
80
Peptide name
Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 41 of Polyamine-transporting ATPase 13A2

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 80 of Polyamine-transporting ATPase 13A2

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 Polyamine-transporting ATPase 13A2 between cysteines 298 and 317.

Details

Redox score ?
71
PDB code
7vpl
Structure name
cryo-em structure of the human atp13a2 (spm-bound e2pi state)
Structure deposition date
2021-10-17
Thiol separation (Å)
3
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
56
Peptide accession
Q9NQ11
Residue number A
298
Residue number B
317
Peptide name
Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 298 of Polyamine-transporting ATPase 13A2

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 317 of Polyamine-transporting ATPase 13A2

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 Isoform 3 of Polyamine-transporting ATPase 13A2 between cysteines 871 and 910.

Details

Redox score ?
61
PDB code
7n75
Structure name
cryo-em structure of atp13a2 d458n/d962n mutant in the e1-apo state, conformation 1
Structure deposition date
2021-06-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
95
Minimum pKa ?
8
% buried
100
Peptide accession
Q9NQ11-3
Residue number A
871
Residue number B
910
Peptide name
Isoform 3 of Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 871 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 910 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 Isoform 3 of Polyamine-transporting ATPase 13A2 between cysteines 1136 and 1140. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
7n75
Structure name
cryo-em structure of atp13a2 d458n/d962n mutant in the e1-apo state, conformation 1
Structure deposition date
2021-06-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
32
Minimum pKa ?
9
% buried
0
Peptide accession
Q9NQ11-3
Residue number A
1136
Residue number B
1140
Peptide name
Isoform 3 of Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 1136 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 1140 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 Isoform 3 of Polyamine-transporting ATPase 13A2 between cysteines 291 and 293. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7n75
Structure name
cryo-em structure of atp13a2 d458n/d962n mutant in the e1-apo state, conformation 1
Structure deposition date
2021-06-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
28
Peptide accession
Q9NQ11-3
Residue number A
291
Residue number B
293
Peptide name
Isoform 3 of Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 291 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 293 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 Isoform 3 of Polyamine-transporting ATPase 13A2 between cysteines 189 and 360. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7n75
Structure name
cryo-em structure of atp13a2 d458n/d962n mutant in the e1-apo state, conformation 1
Structure deposition date
2021-06-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
14
Peptide accession
Q9NQ11-3
Residue number A
189
Residue number B
360
Peptide name
Isoform 3 of Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 189 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 360 of Isoform 3 of Polyamine-transporting ATPase 13A2

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.

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 Isoform 3 of Polyamine-transporting ATPase 13A2 between cysteines 324 and 371. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7n75
Structure name
cryo-em structure of atp13a2 d458n/d962n mutant in the e1-apo state, conformation 1
Structure deposition date
2021-06-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
12
% buried
98
Peptide accession
Q9NQ11-3
Residue number A
324
Residue number B
371
Peptide name
Isoform 3 of Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 324 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 371 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 Isoform 3 of Polyamine-transporting ATPase 13A2 between cysteines 475 and 920. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7n75
Structure name
cryo-em structure of atp13a2 d458n/d962n mutant in the e1-apo state, conformation 1
Structure deposition date
2021-06-09
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
11
% buried
100
Peptide accession
Q9NQ11-3
Residue number A
475
Residue number B
920
Peptide name
Isoform 3 of Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 475 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 920 of Isoform 3 of Polyamine-transporting ATPase 13A2

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 Polyamine-transporting ATPase 13A2 between cysteines 296 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7m5v
Structure name
human atp13a2 in the amppnp-bound occluded state
Structure deposition date
2021-03-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
46
Peptide accession
Q9NQ11
Residue number A
296
Residue number B
317
Peptide name
Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 296 of Polyamine-transporting ATPase 13A2

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 317 of Polyamine-transporting ATPase 13A2

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 Polyamine-transporting ATPase 13A2 between cysteines 329 and 401 (324 and 396 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
7n70
Structure name
cryo-em structure of atp13a2 in the bef-bound e2p-like state
Structure deposition date
2021-06-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
89
Minimum pKa ?
11
% buried
98
Peptide accession
Q9NQ11
Residue number A
329
Residue number B
401
Peptide name
Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 329 of Polyamine-transporting ATPase 13A2

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 401 of Polyamine-transporting ATPase 13A2

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 Polyamine-transporting ATPase 13A2 between cysteines 376 and 401 (371 and 396 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
7n70
Structure name
cryo-em structure of atp13a2 in the bef-bound e2p-like state
Structure deposition date
2021-06-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
98
Peptide accession
Q9NQ11
Residue number A
376
Residue number B
401
Peptide name
Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 376 of Polyamine-transporting ATPase 13A2

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 401 of Polyamine-transporting ATPase 13A2

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 Polyamine-transporting ATPase 13A2 between cysteines 317 and 329 (312 and 324 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
21
PDB code
7n76
Structure name
cryo-em structure of atp13a2 d458n/d962n mutant in the e1-apo state, conformation 2
Structure deposition date
2021-06-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
14
% buried
94
Peptide accession
Q9NQ11
Residue number A
317
Residue number B
329
Peptide name
Polyamine-transporting ATPase 13A2

Ligandability

Cysteine 317 of Polyamine-transporting ATPase 13A2

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 329 of Polyamine-transporting ATPase 13A2

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.

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