ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Prestin

Intramolecular
Cysteine 192 and cysteine 196
Cysteine 124 and cysteine 415
Cysteine 124 and cysteine 381
A redox-regulated disulphide may form within Prestin between cysteines 192 and 196.

Details

Redox score ?
73
PDB code
7sun
Structure name
atomic model of prestin from gerbil (meriones unguiculatus)
Structure deposition date
2021-11-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
0
Peptide accession
Q9JKQ2
Residue number A
192
Residue number B
196
Peptide name
Prestin

Ligandability

Cysteine 192 of Prestin

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 196 of Prestin

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 Prestin between cysteines 124 and 415.

Details

Redox score ?
71
PDB code
7lgu
Structure name
structure of human prestin in the presence of nacl
Structure deposition date
2021-01-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
86
Peptide accession
P58743
Residue number A
124
Residue number B
415
Peptide name
Prestin

Ligandability

Cysteine 124 of Prestin

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 415 of Prestin

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 Prestin between cysteines 124 and 381. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
7lh3
Structure name
structure of human prestin in the presence of sodium sulfate
Structure deposition date
2021-01-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
95
Peptide accession
P58743
Residue number A
124
Residue number B
381
Peptide name
Prestin

Ligandability

Cysteine 124 of Prestin

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 381 of Prestin

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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