ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Bestrophin-2

Intermolecular
Cysteine 108 and cysteine 185
Intramolecular
Cysteine 185 and cysteine 221
Cysteine 99 and cysteine 221
Cysteine 69 and cysteine 251
A redox-regulated disulphide may form between two units of Bestrophin-2 at cysteines 108 and 185. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
8d1f
Structure name
hbest2 5mm ca2+ (ca2+-bound) closed state
Structure deposition date
2022-05-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
100
Minimum pKa ?
11
% buried
100
Peptide A name
Bestrophin-2
Peptide B name
Bestrophin-2
Peptide A accession
Q8NFU1
Peptide B accession
Q8NFU1
Peptide A residue number
108
Peptide B residue number
185

Ligandability

Cysteine 108 of Bestrophin-2

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 185 of Bestrophin-2

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 Bestrophin-2 between cysteines 185 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
8d1g
Structure name
hbest2 ca2+-bound open state
Structure deposition date
2022-05-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
92
Minimum pKa ?
11
% buried
100
Peptide accession
Q8NFU1
Residue number A
185
Residue number B
221
Peptide name
Bestrophin-2

Ligandability

Cysteine 185 of Bestrophin-2

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 221 of Bestrophin-2

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 Bestrophin-2 between cysteines 99 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
8d1h
Structure name
hbest2 ca2+-unbound closed state
Structure deposition date
2022-05-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
89
Peptide accession
Q8NFU1
Residue number A
99
Residue number B
221
Peptide name
Bestrophin-2

Ligandability

Cysteine 99 of Bestrophin-2

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 221 of Bestrophin-2

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 Bestrophin-2 between cysteines 69 and 251. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
8d1g
Structure name
hbest2 ca2+-bound open state
Structure deposition date
2022-05-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
98
Peptide accession
Q8NFU1
Residue number A
69
Residue number B
251
Peptide name
Bestrophin-2

Ligandability

Cysteine 69 of Bestrophin-2

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 251 of Bestrophin-2

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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