ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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All-trans-retinol dehydrogenase [NAD(+)] ADH7

Intramolecular
Cysteine 116 and cysteine 124
Cysteine 110 and cysteine 116
Cysteine 113 and cysteine 124
Cysteine 110 and cysteine 113
Cysteine 110 and cysteine 124
Cysteine 207 and cysteine 223
Cysteine 59 and cysteine 186
Cysteine 113 and cysteine 116
Cysteine 22 and cysteine 144
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 116 and 124 (103 and 111 respectively in this structure).

Details

Redox score ?
91
PDB code
1agn
Structure name
x-ray structure of human sigma alcohol dehydrogenase
Structure deposition date
1996-06-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
68
Minimum pKa ?
3
% buried
52
Peptide accession
P40394
Residue number A
116
Residue number B
124
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 116 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 124 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 110 and 116 (97 and 103 respectively in this structure).

Details

Redox score ?
89
PDB code
1agn
Structure name
x-ray structure of human sigma alcohol dehydrogenase
Structure deposition date
1996-06-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
3
% buried
34
Peptide accession
P40394
Residue number A
110
Residue number B
116
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 110 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 116 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 113 and 124 (100 and 111 respectively in this structure).

Details

Redox score ?
89
PDB code
1agn
Structure name
x-ray structure of human sigma alcohol dehydrogenase
Structure deposition date
1996-06-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
3
% buried
49
Peptide accession
P40394
Residue number A
113
Residue number B
124
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 113 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 124 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 110 and 113 (97 and 100 respectively in this structure).

Details

Redox score ?
78
PDB code
1agn
Structure name
x-ray structure of human sigma alcohol dehydrogenase
Structure deposition date
1996-06-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
34
Peptide accession
P40394
Residue number A
110
Residue number B
113
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 110 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 113 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 110 and 124 (97 and 111 respectively in this structure).

Details

Redox score ?
77
PDB code
1d1t
Structure name
mutant of human sigma alcohol dehydrogenase with leucine at position 141
Structure deposition date
1999-09-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
7
% buried
50
Peptide accession
P40394
Residue number A
110
Residue number B
124
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 110 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 124 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 207 and 223 (195 and 211 respectively in this structure).

Details

Redox score ?
70
PDB code
1agn
Structure name
x-ray structure of human sigma alcohol dehydrogenase
Structure deposition date
1996-06-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
98
Minimum pKa ?
8
% buried
94
Peptide accession
P40394
Residue number A
207
Residue number B
223
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 207 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 59 and 186 (46 and 174 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
1agn
Structure name
x-ray structure of human sigma alcohol dehydrogenase
Structure deposition date
1996-06-04
Thiol separation (Å)
3
Half-sphere exposure sum ?
90
Minimum pKa ?
18
% buried
nan
Peptide accession
P40394
Residue number A
59
Residue number B
186
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 59 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 113 and 116 (100 and 103 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
1d1s
Structure name
wild-type human sigma (class iv) alcohol dehydrogenase
Structure deposition date
1999-09-21
Thiol separation (Å)
3
Half-sphere exposure sum ?
64
Minimum pKa ?
22
% buried
nan
Peptide accession
P40394
Residue number A
113
Residue number B
116
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 113 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 116 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 All-trans-retinol dehydrogenase [NAD(+)] ADH7 between cysteines 22 and 144 (9 and 132 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1d1t
Structure name
mutant of human sigma alcohol dehydrogenase with leucine at position 141
Structure deposition date
1999-09-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
11
% buried
52
Peptide accession
P40394
Residue number A
22
Residue number B
144
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH7

Ligandability

Cysteine 22 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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 144 of All-trans-retinol dehydrogenase [NAD(+)] ADH7

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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