ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Aflatoxin B1 aldehyde reductase member 3

Intramolecular
Cysteine 70 and cysteine 104
Cysteine 154 and cysteine 157
Cysteine 154 and cysteine 186
Cysteine 128 and cysteine 157
A redox-regulated disulphide may form within Aflatoxin B1 aldehyde reductase member 3 between cysteines 70 and 104 (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 ?
51
PDB code
2clp
Structure name
crystal structure of human aflatoxin b1 aldehyde reductase member 3
Structure deposition date
2006-04-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
38
Peptide accession
O95154
Residue number A
70
Residue number B
104
Peptide name
Aflatoxin B1 aldehyde reductase member 3

Ligandability

Cysteine 70 of Aflatoxin B1 aldehyde reductase member 3

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 104 of Aflatoxin B1 aldehyde reductase member 3

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 3 between cysteines 154 and 157 (183 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 ?
48
PDB code
2clp
Structure name
crystal structure of human aflatoxin b1 aldehyde reductase member 3
Structure deposition date
2006-04-28
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
86
Peptide accession
O95154
Residue number A
154
Residue number B
157
Peptide name
Aflatoxin B1 aldehyde reductase member 3

Ligandability

Cysteine 154 of Aflatoxin B1 aldehyde reductase member 3

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 157 of Aflatoxin B1 aldehyde reductase member 3

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 3 between cysteines 154 and 186 (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
2clp
Structure name
crystal structure of human aflatoxin b1 aldehyde reductase member 3
Structure deposition date
2006-04-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
13
% buried
99
Peptide accession
O95154
Residue number A
154
Residue number B
186
Peptide name
Aflatoxin B1 aldehyde reductase member 3

Ligandability

Cysteine 154 of Aflatoxin B1 aldehyde reductase member 3

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 Aflatoxin B1 aldehyde reductase member 3

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 3 between cysteines 128 and 157 (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
2clp
Structure name
crystal structure of human aflatoxin b1 aldehyde reductase member 3
Structure deposition date
2006-04-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
88
Peptide accession
O95154
Residue number A
128
Residue number B
157
Peptide name
Aflatoxin B1 aldehyde reductase member 3

Ligandability

Cysteine 128 of Aflatoxin B1 aldehyde reductase member 3

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 157 of Aflatoxin B1 aldehyde reductase member 3

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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