ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Anoctamin-10

Intramolecular
Cysteine 323 and cysteine 325
Cysteine 513 and cysteine 571
A redox-regulated disulphide may form within Anoctamin-10 between cysteines 323 and 325. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
5oc9
Structure name
crystal structure of human tmem16k / anoctamin 10
Structure deposition date
2017-06-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
36
Peptide accession
Q9NW15
Residue number A
323
Residue number B
325
Peptide name
Anoctamin-10

Ligandability

Cysteine 323 of Anoctamin-10

Cysteine 325 of Anoctamin-10

A redox-regulated disulphide may form within Anoctamin-10 between cysteines 513 and 571. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
5oc9
Structure name
crystal structure of human tmem16k / anoctamin 10
Structure deposition date
2017-06-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
92
Peptide accession
Q9NW15
Residue number A
513
Residue number B
571
Peptide name
Anoctamin-10

Ligandability

Cysteine 513 of Anoctamin-10

Cysteine 571 of Anoctamin-10

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