ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aldehyde dehydrogenase family 1 member A3

Intermolecular
Cysteine 164 and cysteine 467 L
Intramolecular
Cysteine 313 and cysteine 314 L
Cysteine 196 and cysteine 197 L
Cysteine 301 and cysteine 467
Cysteine 52 and cysteine 61
Cysteine 287 and cysteine 301
Cysteine 174 and cysteine 197 L
Cysteine 287 and cysteine 467
A redox-regulated disulphide may form between two units of Aldehyde dehydrogenase family 1 member A3 at cysteines 164 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
5fhz
Structure name
human aldehyde dehydrogenase 1a3 complexed with nad(+) and retinoic acid
Structure deposition date
2015-12-22
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
12
% buried
96
Peptide A name
Aldehyde dehydrogenase family 1 member A3
Peptide B name
Aldehyde dehydrogenase family 1 member A3
Peptide A accession
P47895
Peptide B accession
P47895
Peptide A residue number
164
Peptide B residue number
467

Ligandability

Cysteine 164 of Aldehyde dehydrogenase family 1 member A3

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 467 of Aldehyde dehydrogenase family 1 member A3

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 1 member A3 between cysteines 313 and 314.

Details

Redox score ?
65
PDB code
6tgw
Structure name
crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor
Structure deposition date
2019-11-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
7
% buried
100
Peptide accession
P47895
Residue number A
313
Residue number B
314
Peptide name
Aldehyde dehydrogenase family 1 member A3

Ligandability

Cysteine 313 of Aldehyde dehydrogenase family 1 member A3

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 314 of Aldehyde dehydrogenase family 1 member A3

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Aldehyde dehydrogenase family 1 member A3 between cysteines 196 and 197.

Details

Redox score ?
61
PDB code
5fhz
Structure name
human aldehyde dehydrogenase 1a3 complexed with nad(+) and retinoic acid
Structure deposition date
2015-12-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
95
Minimum pKa ?
9
% buried
100
Peptide accession
P47895
Residue number A
196
Residue number B
197
Peptide name
Aldehyde dehydrogenase family 1 member A3

Ligandability

Cysteine 196 of Aldehyde dehydrogenase family 1 member A3

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 197 of Aldehyde dehydrogenase family 1 member A3

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Aldehyde dehydrogenase family 1 member A3 between cysteines 301 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7qk8
Structure name
crystal structure of the aldh1a3-nad+ complex
Structure deposition date
2021-12-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
78
Peptide accession
P47895
Residue number A
301
Residue number B
467
Peptide name
Aldehyde dehydrogenase family 1 member A3

Ligandability

Cysteine 301 of Aldehyde dehydrogenase family 1 member A3

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 467 of Aldehyde dehydrogenase family 1 member A3

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 1 member A3 between cysteines 52 and 61. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6tgw
Structure name
crystal structure of human aldehyde dehydrogenase 1a3 in complex with a selective inhibitor
Structure deposition date
2019-11-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
34
Peptide accession
P47895
Residue number A
52
Residue number B
61
Peptide name
Aldehyde dehydrogenase family 1 member A3

Ligandability

Cysteine 52 of Aldehyde dehydrogenase family 1 member A3

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 61 of Aldehyde dehydrogenase family 1 member A3

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 1 member A3 between cysteines 287 and 301. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7qk8
Structure name
crystal structure of the aldh1a3-nad+ complex
Structure deposition date
2021-12-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
86
Peptide accession
P47895
Residue number A
287
Residue number B
301
Peptide name
Aldehyde dehydrogenase family 1 member A3

Ligandability

Cysteine 287 of Aldehyde dehydrogenase family 1 member A3

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 301 of Aldehyde dehydrogenase family 1 member A3

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 1 member A3 between cysteines 174 and 197. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6try
Structure name
crystal structure of human aldehyde dehydrogenase 1a3 in complex with mf13 inhibitor compound
Structure deposition date
2019-12-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
100
Peptide accession
P47895
Residue number A
174
Residue number B
197
Peptide name
Aldehyde dehydrogenase family 1 member A3

Ligandability

Cysteine 174 of Aldehyde dehydrogenase family 1 member A3

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 197 of Aldehyde dehydrogenase family 1 member A3

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Aldehyde dehydrogenase family 1 member A3 between cysteines 287 and 467. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
19
PDB code
5fhz
Structure name
human aldehyde dehydrogenase 1a3 complexed with nad(+) and retinoic acid
Structure deposition date
2015-12-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
93
Minimum pKa ?
12
% buried
100
Peptide accession
P47895
Residue number A
287
Residue number B
467
Peptide name
Aldehyde dehydrogenase family 1 member A3

Ligandability

Cysteine 287 of Aldehyde dehydrogenase family 1 member A3

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 467 of Aldehyde dehydrogenase family 1 member A3

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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