ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ADP-sugar pyrophosphatase

Intermolecular
Cysteine 131 and cysteine 91
Cysteine 76 and cysteine 126
Intramolecular
Cysteine 131 and cysteine 139
A redox-regulated disulphide may form between two units of ADP-sugar pyrophosphatase at cysteines 131 and 91.

Details

Redox score ?
65
PDB code
5qj9
Structure name
pandda analysis group deposition of models with modelled events (e
Structure deposition date
2018-11-12
Thiol separation (Å)
4
Half-sphere exposure sum ?
86
Minimum pKa ?
10
% buried
98
Peptide A name
ADP-sugar pyrophosphatase
Peptide B name
ADP-sugar pyrophosphatase
Peptide A accession
Q9UKK9
Peptide B accession
Q9UKK9
Peptide A residue number
131
Peptide B residue number
91

Ligandability

Cysteine 131 of ADP-sugar pyrophosphatase

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 91 of ADP-sugar pyrophosphatase

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 between two units of ADP-sugar pyrophosphatase at cysteines 76 and 126. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2dsb
Structure name
crystal structure of human adp-ribose pyrophosphatase nudt5
Structure deposition date
2006-06-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
90
Peptide A name
ADP-sugar pyrophosphatase
Peptide B name
ADP-sugar pyrophosphatase
Peptide A accession
Q9UKK9
Peptide B accession
Q9UKK9
Peptide A residue number
76
Peptide B residue number
126

Ligandability

Cysteine 76 of ADP-sugar pyrophosphatase

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 126 of ADP-sugar pyrophosphatase

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 ADP-sugar pyrophosphatase between cysteines 131 and 139. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
5nqr
Structure name
potent inhibitors of nudt5 silence hormone signaling in breast cancer
Structure deposition date
2017-04-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
10
% buried
100
Peptide accession
Q9UKK9
Residue number A
131
Residue number B
139
Peptide name
ADP-sugar pyrophosphatase

Ligandability

Cysteine 131 of ADP-sugar pyrophosphatase

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 139 of ADP-sugar pyrophosphatase

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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