ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Phospholipid-transporting ATPase

Intramolecular
Cysteine 871 and cysteine 875
Cysteine 78 and cysteine 249
Cysteine 500 and cysteine 584
Cysteine 786 and cysteine 787
Cysteine 781 and cysteine 786
Cysteine 584 and cysteine 621
A redox-regulated disulphide may form within Phospholipid-transporting ATPase between cysteines 871 and 875 (843 and 847 respectively in this structure).

Details

Redox score ?
65
PDB code
6k7j
Structure name
cryo-em structure of the human p4-type flippase atp8a1-cdc50 (e1-atp state class1)
Structure deposition date
2019-06-07
Thiol separation (Å)
5
Half-sphere exposure sum ?
89
Minimum pKa ?
8
% buried
100
Peptide accession
Q59EX4
Residue number A
871
Residue number B
875
Peptide name
Phospholipid-transporting ATPase

Ligandability

Cysteine 871 of Phospholipid-transporting ATPase

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 875 of Phospholipid-transporting ATPase

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 Phospholipid-transporting ATPase between cysteines 78 and 249 (50 and 221 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6k7i
Structure name
cryo-em structure of the human p4-type flippase atp8a1-cdc50 (e1-atp state class2)
Structure deposition date
2019-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
32
Peptide accession
Q59EX4
Residue number A
78
Residue number B
249
Peptide name
Phospholipid-transporting ATPase

Ligandability

Cysteine 78 of Phospholipid-transporting ATPase

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 249 of Phospholipid-transporting ATPase

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 Phospholipid-transporting ATPase between cysteines 500 and 584 (472 and 556 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6k7j
Structure name
cryo-em structure of the human p4-type flippase atp8a1-cdc50 (e1-atp state class1)
Structure deposition date
2019-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
Q59EX4
Residue number A
500
Residue number B
584
Peptide name
Phospholipid-transporting ATPase

Ligandability

Cysteine 500 of Phospholipid-transporting ATPase

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 584 of Phospholipid-transporting ATPase

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 Phospholipid-transporting ATPase between cysteines 786 and 787 (758 and 759 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
6k7l
Structure name
cryo-em structure of the human p4-type flippase atp8a1-cdc50 (e2p state class2)
Structure deposition date
2019-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
97
Peptide accession
Q59EX4
Residue number A
786
Residue number B
787
Peptide name
Phospholipid-transporting ATPase

Ligandability

Cysteine 786 of Phospholipid-transporting ATPase

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 787 of Phospholipid-transporting ATPase

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 Phospholipid-transporting ATPase between cysteines 781 and 786 (753 and 758 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6k7g
Structure name
cryo-em structure of the human p4-type flippase atp8a1-cdc50 (e1 state class1)
Structure deposition date
2019-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
78
Peptide accession
Q59EX4
Residue number A
781
Residue number B
786
Peptide name
Phospholipid-transporting ATPase

Ligandability

Cysteine 781 of Phospholipid-transporting ATPase

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 786 of Phospholipid-transporting ATPase

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 Phospholipid-transporting ATPase between cysteines 584 and 621 (556 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 ?
21
PDB code
6k7l
Structure name
cryo-em structure of the human p4-type flippase atp8a1-cdc50 (e2p state class2)
Structure deposition date
2019-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
96
Minimum pKa ?
13
% buried
100
Peptide accession
Q59EX4
Residue number A
584
Residue number B
621
Peptide name
Phospholipid-transporting ATPase

Ligandability

Cysteine 584 of Phospholipid-transporting ATPase

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 621 of Phospholipid-transporting ATPase

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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