ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aldehyde dehydrogenase, dimeric NADP-preferring

Intramolecular
Cysteine 252 and cysteine 344
Cysteine 223 and cysteine 229
Cysteine 217 and cysteine 223
Cysteine 229 and cysteine 252
Cysteine 223 and cysteine 252
Cysteine 217 and cysteine 229
Cysteine 217 and cysteine 252
A redox-regulated disulphide may form within Aldehyde dehydrogenase, dimeric NADP-preferring between cysteines 252 and 344 (251 and 343 respectively in this structure).

Details

Redox score ?
71
PDB code
3sza
Structure name
crystal structure of human aldh3a1 - apo form
Structure deposition date
2011-07-18
Thiol separation (Å)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
7
% buried
61
Peptide accession
P30838
Residue number A
252
Residue number B
344
Peptide name
Aldehyde dehydrogenase, dimeric NADP-preferring

Ligandability

Cysteine 252 of Aldehyde dehydrogenase, dimeric NADP-preferring

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 344 of Aldehyde dehydrogenase, dimeric NADP-preferring

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, dimeric NADP-preferring between cysteines 223 and 229 (222 and 228 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4l2o
Structure name
crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
Structure deposition date
2013-06-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
12
% buried
84
Peptide accession
P30838
Residue number A
223
Residue number B
229
Peptide name
Aldehyde dehydrogenase, dimeric NADP-preferring

Ligandability

Cysteine 223 of Aldehyde dehydrogenase, dimeric NADP-preferring

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 229 of Aldehyde dehydrogenase, dimeric NADP-preferring

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, dimeric NADP-preferring between cysteines 217 and 223 (216 and 222 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4l2o
Structure name
crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
Structure deposition date
2013-06-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
84
Peptide accession
P30838
Residue number A
217
Residue number B
223
Peptide name
Aldehyde dehydrogenase, dimeric NADP-preferring

Ligandability

Cysteine 217 of Aldehyde dehydrogenase, dimeric NADP-preferring

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 223 of Aldehyde dehydrogenase, dimeric NADP-preferring

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, dimeric NADP-preferring between cysteines 229 and 252 (228 and 251 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4h80
Structure name
crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
Structure deposition date
2012-09-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
12
% buried
88
Peptide accession
P30838
Residue number A
229
Residue number B
252
Peptide name
Aldehyde dehydrogenase, dimeric NADP-preferring

Ligandability

Cysteine 229 of Aldehyde dehydrogenase, dimeric NADP-preferring

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 252 of Aldehyde dehydrogenase, dimeric NADP-preferring

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, dimeric NADP-preferring between cysteines 223 and 252 (222 and 251 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4l2o
Structure name
crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
Structure deposition date
2013-06-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
12
% buried
74
Peptide accession
P30838
Residue number A
223
Residue number B
252
Peptide name
Aldehyde dehydrogenase, dimeric NADP-preferring

Ligandability

Cysteine 223 of Aldehyde dehydrogenase, dimeric NADP-preferring

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 252 of Aldehyde dehydrogenase, dimeric NADP-preferring

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, dimeric NADP-preferring between cysteines 217 and 229 (216 and 228 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4h80
Structure name
crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
Structure deposition date
2012-09-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
99
Peptide accession
P30838
Residue number A
217
Residue number B
229
Peptide name
Aldehyde dehydrogenase, dimeric NADP-preferring

Ligandability

Cysteine 217 of Aldehyde dehydrogenase, dimeric NADP-preferring

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 229 of Aldehyde dehydrogenase, dimeric NADP-preferring

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, dimeric NADP-preferring between cysteines 217 and 252 (216 and 251 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
4l1o
Structure name
crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione
Structure deposition date
2013-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
89
Peptide accession
P30838
Residue number A
217
Residue number B
252
Peptide name
Aldehyde dehydrogenase, dimeric NADP-preferring

Ligandability

Cysteine 217 of Aldehyde dehydrogenase, dimeric NADP-preferring

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 252 of Aldehyde dehydrogenase, dimeric NADP-preferring

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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