ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Anoctamin-1

Intramolecular
Cysteine 379 and cysteine 836
Cysteine 379 and cysteine 382
Cysteine 382 and cysteine 386
Cysteine 625 and cysteine 630
Cysteine 625 and cysteine 635
Cysteine 370 and cysteine 395
Cysteine 630 and cysteine 635
A redox-regulated disulphide may form within Anoctamin-1 between cysteines 379 and 836.

Details

Redox score ?
82
PDB code
5oyb
Structure name
structure of calcium-bound mtmem16a chloride channel at 3
Structure deposition date
2017-09-08
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8BHY3
Residue number A
379
Residue number B
836
Peptide name
Anoctamin-1

Ligandability

Cysteine 379 of Anoctamin-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 836 of Anoctamin-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 Anoctamin-1 between cysteines 379 and 382.

Details

Redox score ?
63
PDB code
6bgi
Structure name
cryo-em structure of the tmem16a calcium-activated chloride channel in nanodisc
Structure deposition date
2017-10-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
13
Peptide accession
Q8BHY3
Residue number A
379
Residue number B
382
Peptide name
Anoctamin-1

Ligandability

Cysteine 379 of Anoctamin-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 382 of Anoctamin-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 Anoctamin-1 between cysteines 382 and 386. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
6bgj
Structure name
cryo-em structure of the tmem16a calcium-activated chloride channel in lmng
Structure deposition date
2017-10-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
10
% buried
2
Peptide accession
Q8BHY3
Residue number A
382
Residue number B
386
Peptide name
Anoctamin-1

Ligandability

Cysteine 382 of Anoctamin-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 386 of Anoctamin-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 Anoctamin-1 between cysteines 625 and 630 (621 and 626 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
6bgi
Structure name
cryo-em structure of the tmem16a calcium-activated chloride channel in nanodisc
Structure deposition date
2017-10-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
9
% buried
57
Peptide accession
Q8BHY3
Residue number A
625
Residue number B
630
Peptide name
Anoctamin-1

Ligandability

Cysteine 625 of Anoctamin-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 630 of Anoctamin-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 Anoctamin-1 between cysteines 625 and 635 (621 and 631 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6bgi
Structure name
cryo-em structure of the tmem16a calcium-activated chloride channel in nanodisc
Structure deposition date
2017-10-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
61
Peptide accession
Q8BHY3
Residue number A
625
Residue number B
635
Peptide name
Anoctamin-1

Ligandability

Cysteine 625 of Anoctamin-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 635 of Anoctamin-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 Anoctamin-1 between cysteines 370 and 395. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6bgj
Structure name
cryo-em structure of the tmem16a calcium-activated chloride channel in lmng
Structure deposition date
2017-10-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
60
Peptide accession
Q8BHY3
Residue number A
370
Residue number B
395
Peptide name
Anoctamin-1

Ligandability

Cysteine 370 of Anoctamin-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 395 of Anoctamin-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 Anoctamin-1 between cysteines 630 and 635 (626 and 631 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6bgj
Structure name
cryo-em structure of the tmem16a calcium-activated chloride channel in lmng
Structure deposition date
2017-10-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
87
Peptide accession
Q8BHY3
Residue number A
630
Residue number B
635
Peptide name
Anoctamin-1

Ligandability

Cysteine 630 of Anoctamin-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 635 of Anoctamin-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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