ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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UDP-glucose 6-dehydrogenase

Intramolecular
Cysteine 9 and cysteine 20
Cysteine 27 and cysteine 64
Cysteine 9 and cysteine 112
Cysteine 8 and cysteine 9
Cysteine 20 and cysteine 64
Cysteine 8 and cysteine 112
Cysteine 8 and cysteine 20
A redox-regulated disulphide may form within UDP-glucose 6-dehydrogenase between cysteines 9 and 20.

Details

Redox score ?
69
PDB code
6c4j
Structure name
ligand bound full length hugdh with a104l substitution
Structure deposition date
2018-01-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
98
Minimum pKa ?
8
% buried
100
Peptide accession
O60701
Residue number A
9
Residue number B
20
Peptide name
UDP-glucose 6-dehydrogenase

Ligandability

Cysteine 9 of UDP-glucose 6-dehydrogenase

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 20 of UDP-glucose 6-dehydrogenase

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 UDP-glucose 6-dehydrogenase between cysteines 27 and 64. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6c4j
Structure name
ligand bound full length hugdh with a104l substitution
Structure deposition date
2018-01-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
48
Peptide accession
O60701
Residue number A
27
Residue number B
64
Peptide name
UDP-glucose 6-dehydrogenase

Ligandability

Cysteine 27 of UDP-glucose 6-dehydrogenase

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 64 of UDP-glucose 6-dehydrogenase

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 UDP-glucose 6-dehydrogenase between cysteines 9 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6c5z
Structure name
human udp-glucose dehydrogenase a225l substitutuion with udp-glucose and nadh bound
Structure deposition date
2018-01-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
8
% buried
100
Peptide accession
O60701
Residue number A
9
Residue number B
112
Peptide name
UDP-glucose 6-dehydrogenase

Ligandability

Cysteine 9 of UDP-glucose 6-dehydrogenase

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 112 of UDP-glucose 6-dehydrogenase

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 UDP-glucose 6-dehydrogenase between cysteines 8 and 9. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6c4k
Structure name
full length hugdh with a104l substitution in the absence of ligand
Structure deposition date
2018-01-12
Thiol separation (Å)
7
Half-sphere exposure sum ?
97
Minimum pKa ?
13
% buried
97
Peptide accession
O60701
Residue number A
8
Residue number B
9
Peptide name
UDP-glucose 6-dehydrogenase

Ligandability

Cysteine 8 of UDP-glucose 6-dehydrogenase

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 9 of UDP-glucose 6-dehydrogenase

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 UDP-glucose 6-dehydrogenase between cysteines 20 and 64. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4edf
Structure name
dimeric hugdh, k94e
Structure deposition date
2012-03-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
76
Peptide accession
O60701
Residue number A
20
Residue number B
64
Peptide name
UDP-glucose 6-dehydrogenase

Ligandability

Cysteine 20 of UDP-glucose 6-dehydrogenase

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 64 of UDP-glucose 6-dehydrogenase

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 UDP-glucose 6-dehydrogenase between cysteines 8 and 112. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
3itk
Structure name
crystal structure of human udp-glucose dehydrogenase thr131ala, apo form
Structure deposition date
2009-08-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
97
Peptide accession
O60701
Residue number A
8
Residue number B
112
Peptide name
UDP-glucose 6-dehydrogenase

Ligandability

Cysteine 8 of UDP-glucose 6-dehydrogenase

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 112 of UDP-glucose 6-dehydrogenase

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 UDP-glucose 6-dehydrogenase between cysteines 8 and 20. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3tf5
Structure name
structure of udp-glucose dehydrogenase v132 deletion
Structure deposition date
2011-08-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
98
Minimum pKa ?
13
% buried
100
Peptide accession
O60701
Residue number A
8
Residue number B
20
Peptide name
UDP-glucose 6-dehydrogenase

Ligandability

Cysteine 8 of UDP-glucose 6-dehydrogenase

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 20 of UDP-glucose 6-dehydrogenase

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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