ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aldehyde dehydrogenase family 3 member A2

Intramolecular
Cysteine 220 and cysteine 226
Cysteine 50 and cysteine 237
Cysteine 220 and cysteine 249
Cysteine 226 and cysteine 249
Cysteine 214 and cysteine 220
Cysteine 214 and cysteine 226
Cysteine 214 and cysteine 249
A redox-regulated disulphide may form within Aldehyde dehydrogenase family 3 member A2 between cysteines 220 and 226. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4qgk
Structure name
structure of the human sjogren larsson syndrome enzyme fatty aldehyde dehydrogenase (faldh)
Structure deposition date
2014-05-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
12
% buried
80
Peptide accession
P51648
Residue number A
220
Residue number B
226
Peptide name
Aldehyde dehydrogenase family 3 member A2

Ligandability

Cysteine 220 of Aldehyde dehydrogenase family 3 member A2

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 226 of Aldehyde dehydrogenase family 3 member A2

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 Aldehyde dehydrogenase family 3 member A2 between cysteines 50 and 237. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4qgk
Structure name
structure of the human sjogren larsson syndrome enzyme fatty aldehyde dehydrogenase (faldh)
Structure deposition date
2014-05-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
10
% buried
80
Peptide accession
P51648
Residue number A
50
Residue number B
237
Peptide name
Aldehyde dehydrogenase family 3 member A2

Ligandability

Cysteine 50 of Aldehyde dehydrogenase family 3 member A2

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 237 of Aldehyde dehydrogenase family 3 member A2

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 Aldehyde dehydrogenase family 3 member A2 between cysteines 220 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4qgk
Structure name
structure of the human sjogren larsson syndrome enzyme fatty aldehyde dehydrogenase (faldh)
Structure deposition date
2014-05-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
72
Peptide accession
P51648
Residue number A
220
Residue number B
249
Peptide name
Aldehyde dehydrogenase family 3 member A2

Ligandability

Cysteine 220 of Aldehyde dehydrogenase family 3 member A2

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 249 of Aldehyde dehydrogenase family 3 member A2

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 Aldehyde dehydrogenase family 3 member A2 between cysteines 226 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4qgk
Structure name
structure of the human sjogren larsson syndrome enzyme fatty aldehyde dehydrogenase (faldh)
Structure deposition date
2014-05-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
91
Peptide accession
P51648
Residue number A
226
Residue number B
249
Peptide name
Aldehyde dehydrogenase family 3 member A2

Ligandability

Cysteine 226 of Aldehyde dehydrogenase family 3 member A2

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 249 of Aldehyde dehydrogenase family 3 member A2

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 Aldehyde dehydrogenase family 3 member A2 between cysteines 214 and 220. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4qgk
Structure name
structure of the human sjogren larsson syndrome enzyme fatty aldehyde dehydrogenase (faldh)
Structure deposition date
2014-05-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
80
Peptide accession
P51648
Residue number A
214
Residue number B
220
Peptide name
Aldehyde dehydrogenase family 3 member A2

Ligandability

Cysteine 214 of Aldehyde dehydrogenase family 3 member A2

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 220 of Aldehyde dehydrogenase family 3 member A2

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 Aldehyde dehydrogenase family 3 member A2 between cysteines 214 and 226. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
4qgk
Structure name
structure of the human sjogren larsson syndrome enzyme fatty aldehyde dehydrogenase (faldh)
Structure deposition date
2014-05-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
100
Peptide accession
P51648
Residue number A
214
Residue number B
226
Peptide name
Aldehyde dehydrogenase family 3 member A2

Ligandability

Cysteine 214 of Aldehyde dehydrogenase family 3 member A2

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 226 of Aldehyde dehydrogenase family 3 member A2

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 Aldehyde dehydrogenase family 3 member A2 between cysteines 214 and 249. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
4qgk
Structure name
structure of the human sjogren larsson syndrome enzyme fatty aldehyde dehydrogenase (faldh)
Structure deposition date
2014-05-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
91
Peptide accession
P51648
Residue number A
214
Residue number B
249
Peptide name
Aldehyde dehydrogenase family 3 member A2

Ligandability

Cysteine 214 of Aldehyde dehydrogenase family 3 member A2

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 249 of Aldehyde dehydrogenase family 3 member A2

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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