ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Uridine phosphorylase 2

Intramolecular
Cysteine 137 and cysteine 138
Cysteine 95 and cysteine 102
Cysteine 264 and cysteine 267
Cysteine 215 and cysteine 275
A redox-regulated disulphide may form within Uridine phosphorylase 2 between cysteines 137 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
3p0e
Structure name
structure of hupp2 in an active conformation with bound 5- benzylacyclouridine
Structure deposition date
2010-09-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
28
Peptide accession
O95045
Residue number A
137
Residue number B
138
Peptide name
Uridine phosphorylase 2

Ligandability

Cysteine 137 of Uridine phosphorylase 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 138 of Uridine phosphorylase 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 Uridine phosphorylase 2 between cysteines 95 and 102. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3p0e
Structure name
structure of hupp2 in an active conformation with bound 5- benzylacyclouridine
Structure deposition date
2010-09-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
72
Peptide accession
O95045
Residue number A
95
Residue number B
102
Peptide name
Uridine phosphorylase 2

Ligandability

Cysteine 95 of Uridine phosphorylase 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 102 of Uridine phosphorylase 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 Uridine phosphorylase 2 between cysteines 264 and 267. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
3p0e
Structure name
structure of hupp2 in an active conformation with bound 5- benzylacyclouridine
Structure deposition date
2010-09-28
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
92
Peptide accession
O95045
Residue number A
264
Residue number B
267
Peptide name
Uridine phosphorylase 2

Ligandability

Cysteine 264 of Uridine phosphorylase 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 267 of Uridine phosphorylase 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 Uridine phosphorylase 2 between cysteines 215 and 275. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
3p0e
Structure name
structure of hupp2 in an active conformation with bound 5- benzylacyclouridine
Structure deposition date
2010-09-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
94
Minimum pKa ?
12
% buried
100
Peptide accession
O95045
Residue number A
215
Residue number B
275
Peptide name
Uridine phosphorylase 2

Ligandability

Cysteine 215 of Uridine phosphorylase 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 275 of Uridine phosphorylase 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.

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