ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aldehyde dehydrogenase 1A1

Intramolecular
Cysteine 302 and cysteine 303
Cysteine 133 and cysteine 186
Cysteine 163 and cysteine 186
Cysteine 276 and cysteine 456
Cysteine 456 and cysteine 464
A redox-regulated disulphide may form within Aldehyde dehydrogenase 1A1 between cysteines 302 and 303 (301 and 302 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5ac1
Structure name
sheep aldehyde dehydrogenase 1a1 with duocarmycin analog inhibitor
Structure deposition date
2015-08-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
83
Minimum pKa ?
15
% buried
100
Peptide accession
P51977
Residue number A
302
Residue number B
303
Peptide name
Aldehyde dehydrogenase 1A1

Ligandability

Cysteine 302 of Aldehyde dehydrogenase 1A1

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 303 of Aldehyde dehydrogenase 1A1

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 1A1 between cysteines 133 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5l2o
Structure name
crystal structure of aldh1a1 in complex with buc22
Structure deposition date
2016-08-02
Thiol separation (Å)
8
Half-sphere exposure sum ?
102
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00352
Residue number A
133
Residue number B
186
Peptide name
Aldehyde dehydrogenase 1A1

Ligandability

Cysteine 133 of Aldehyde dehydrogenase 1A1

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 186 of Aldehyde dehydrogenase 1A1

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 1A1 between cysteines 163 and 186. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5l2o
Structure name
crystal structure of aldh1a1 in complex with buc22
Structure deposition date
2016-08-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00352
Residue number A
163
Residue number B
186
Peptide name
Aldehyde dehydrogenase 1A1

Ligandability

Cysteine 163 of Aldehyde dehydrogenase 1A1

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 186 of Aldehyde dehydrogenase 1A1

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 1A1 between cysteines 276 and 456. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
5ac2
Structure name
human aldehyde dehydrogenase 1a1 with duocarmycin analog
Structure deposition date
2015-08-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
P00352
Residue number A
276
Residue number B
456
Peptide name
Aldehyde dehydrogenase 1A1

Ligandability

Cysteine 276 of Aldehyde dehydrogenase 1A1

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 456 of Aldehyde dehydrogenase 1A1

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 1A1 between cysteines 456 and 464. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
8d46
Structure name
cryo-electron microscopy structure of human kidney aldehyde dehydrogenase 1a1
Structure deposition date
2022-06-01
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
100
Peptide accession
P00352
Residue number A
456
Residue number B
464
Peptide name
Aldehyde dehydrogenase 1A1

Ligandability

Cysteine 456 of Aldehyde dehydrogenase 1A1

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 464 of Aldehyde dehydrogenase 1A1

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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