ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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UDP-glucose 4-epimerase

Intramolecular
Cysteine 172 and cysteine 264
Cysteine 262 and cysteine 264
Cysteine 172 and cysteine 262
A redox-regulated disulphide may form within UDP-glucose 4-epimerase between cysteines 172 and 264.

Details

Redox score ?
71
PDB code
1i3l
Structure name
molecular basis for severe epimerase-deficiency galactosemia: x-ray structure of the human v94m-substituted udp-galactose 4-epimerase
Structure deposition date
2001-02-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
8
% buried
84
Peptide accession
Q14376
Residue number A
172
Residue number B
264
Peptide name
UDP-glucose 4-epimerase

Ligandability

Cysteine 172 of UDP-glucose 4-epimerase

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 264 of UDP-glucose 4-epimerase

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 4-epimerase between cysteines 262 and 264. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
1i3k
Structure name
molecular basis for severe epimerase-deficiency galactosemia: x-ray structure of the human v94m-substituted udp-galactose 4-epimerase
Structure deposition date
2001-02-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
8
% buried
72
Peptide accession
Q14376
Residue number A
262
Residue number B
264
Peptide name
UDP-glucose 4-epimerase

Ligandability

Cysteine 262 of UDP-glucose 4-epimerase

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 264 of UDP-glucose 4-epimerase

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 4-epimerase between cysteines 172 and 262. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
1ek5
Structure name
structure of human udp-galactose 4-epimerase in complex with nad+
Structure deposition date
2000-03-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
11
% buried
54
Peptide accession
Q14376
Residue number A
172
Residue number B
262
Peptide name
UDP-glucose 4-epimerase

Ligandability

Cysteine 172 of UDP-glucose 4-epimerase

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 262 of UDP-glucose 4-epimerase

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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