ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aflatoxin B1 aldehyde reductase member 2

Intramolecular
Cysteine 98 and cysteine 132
Cysteine 190 and cysteine 193
Cysteine 182 and cysteine 214
Cysteine 156 and cysteine 185
Cysteine 222 and cysteine 193
A redox-regulated disulphide may form within Aflatoxin B1 aldehyde reductase member 2 between cysteines 98 and 132 (99 and 133 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2bp1
Structure name
structure of the aflatoxin aldehyde reductase in complex with nadph
Structure deposition date
2005-04-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
45
Peptide accession
O43488
Residue number A
98
Residue number B
132
Peptide name
Aflatoxin B1 aldehyde reductase member 2

Ligandability

Cysteine 98 of Aflatoxin B1 aldehyde reductase member 2

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 132 of Aflatoxin B1 aldehyde reductase member 2

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 Aflatoxin B1 aldehyde reductase member 2 between cysteines 190 and 193 (150 and 153 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2c91
Structure name
mouse succinic semialdehyde reductase, akr7a5
Structure deposition date
2005-12-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
89
Peptide accession
Q8CG76
Residue number A
190
Residue number B
193
Peptide name
Aflatoxin B1 aldehyde reductase member 2

Ligandability

Cysteine 190 of Aflatoxin B1 aldehyde reductase member 2

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 193 of Aflatoxin B1 aldehyde reductase member 2

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 Aflatoxin B1 aldehyde reductase member 2 between cysteines 182 and 214 (183 and 215 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
2bp1
Structure name
structure of the aflatoxin aldehyde reductase in complex with nadph
Structure deposition date
2005-04-17
Thiol separation (Å)
7
Half-sphere exposure sum ?
76
Minimum pKa ?
13
% buried
98
Peptide accession
O43488
Residue number A
182
Residue number B
214
Peptide name
Aflatoxin B1 aldehyde reductase member 2

Ligandability

Cysteine 182 of Aflatoxin B1 aldehyde reductase member 2

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 214 of Aflatoxin B1 aldehyde reductase member 2

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 Aflatoxin B1 aldehyde reductase member 2 between cysteines 156 and 185 (157 and 186 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2bp1
Structure name
structure of the aflatoxin aldehyde reductase in complex with nadph
Structure deposition date
2005-04-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
88
Peptide accession
O43488
Residue number A
156
Residue number B
185
Peptide name
Aflatoxin B1 aldehyde reductase member 2

Ligandability

Cysteine 156 of Aflatoxin B1 aldehyde reductase member 2

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 185 of Aflatoxin B1 aldehyde reductase member 2

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 Aflatoxin B1 aldehyde reductase member 2 between cysteines 222 and 193 (122 and 153 respectively in this structure).

Details

Redox score ?
nan
PDB code
2c91
Structure name
mouse succinic semialdehyde reductase, akr7a5
Structure deposition date
2005-12-08
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
44
Peptide accession
Q8CG76
Residue number A
222
Residue number B
193
Peptide name
Aflatoxin B1 aldehyde reductase member 2

Ligandability

Cysteine 222 of Aflatoxin B1 aldehyde reductase member 2

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 193 of Aflatoxin B1 aldehyde reductase member 2

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.

Uncertain whether structure cysteine 122 has been assigned to correct residue.
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