ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Retinoid isomerohydrolase

Intramolecular
Cysteine 169 and cysteine 195
Cysteine 45 and cysteine 146
Cysteine 195 and cysteine 231
Cysteine 106 and cysteine 278
Cysteine 329 and cysteine 330
A redox-regulated disulphide may form within Retinoid isomerohydrolase between cysteines 169 and 195. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7k8g
Structure name
crystal structure of bovine rpe65 in complex with 4-fluoro-mb-004 and palmitate
Structure deposition date
2020-09-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
26
Peptide accession
Q28175
Residue number A
169
Residue number B
195
Peptide name
Retinoid isomerohydrolase

Ligandability

Cysteine 169 of Retinoid isomerohydrolase

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 195 of Retinoid isomerohydrolase

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 Retinoid isomerohydrolase between cysteines 45 and 146. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4f3d
Structure name
structure of rpe65: p65 crystal form grown in fos-choline-10
Structure deposition date
2012-05-09
Thiol separation (Å)
7
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
Q28175
Residue number A
45
Residue number B
146
Peptide name
Retinoid isomerohydrolase

Ligandability

Cysteine 45 of Retinoid isomerohydrolase

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 146 of Retinoid isomerohydrolase

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 Retinoid isomerohydrolase between cysteines 195 and 231. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4ryx
Structure name
crystal structure of rpe65 in complex with emixustat and palmitate, p6522 crystal form
Structure deposition date
2014-12-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
56
Peptide accession
Q28175
Residue number A
195
Residue number B
231
Peptide name
Retinoid isomerohydrolase

Ligandability

Cysteine 195 of Retinoid isomerohydrolase

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 231 of Retinoid isomerohydrolase

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 Retinoid isomerohydrolase between cysteines 106 and 278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
3fsn
Structure name
crystal structure of rpe65 at 2
Structure deposition date
2009-01-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q28175
Residue number A
106
Residue number B
278
Peptide name
Retinoid isomerohydrolase

Ligandability

Cysteine 106 of Retinoid isomerohydrolase

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 278 of Retinoid isomerohydrolase

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 Retinoid isomerohydrolase between cysteines 329 and 330. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3kvc
Structure name
crystal structure of bovine rpe65 at 1
Structure deposition date
2009-11-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
Q28175
Residue number A
329
Residue number B
330
Peptide name
Retinoid isomerohydrolase

Ligandability

Cysteine 329 of Retinoid isomerohydrolase

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 330 of Retinoid isomerohydrolase

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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