ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ADP-ribose glycohydrolase MACROD2

Intramolecular
Cysteine 123 and cysteine 164
Cysteine 112 and cysteine 132
Cysteine 117 and cysteine 123
Cysteine 184 and cysteine 222
A redox-regulated disulphide may form within ADP-ribose glycohydrolase MACROD2 between cysteines 123 and 164. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
4iqy
Structure name
crystal structure of the human protein-proximal adp-ribosyl-hydrolase macrod2
Structure deposition date
2013-01-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
11
% buried
74
Peptide accession
A1Z1Q3
Residue number A
123
Residue number B
164
Peptide name
ADP-ribose glycohydrolase MACROD2

Ligandability

Cysteine 123 of ADP-ribose glycohydrolase MACROD2

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 164 of ADP-ribose glycohydrolase MACROD2

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-ribose glycohydrolase MACROD2 between cysteines 112 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4iqy
Structure name
crystal structure of the human protein-proximal adp-ribosyl-hydrolase macrod2
Structure deposition date
2013-01-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
45
Peptide accession
A1Z1Q3
Residue number A
112
Residue number B
132
Peptide name
ADP-ribose glycohydrolase MACROD2

Ligandability

Cysteine 112 of ADP-ribose glycohydrolase MACROD2

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 132 of ADP-ribose glycohydrolase MACROD2

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-ribose glycohydrolase MACROD2 between cysteines 117 and 123. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4iqy
Structure name
crystal structure of the human protein-proximal adp-ribosyl-hydrolase macrod2
Structure deposition date
2013-01-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
62
Peptide accession
A1Z1Q3
Residue number A
117
Residue number B
123
Peptide name
ADP-ribose glycohydrolase MACROD2

Ligandability

Cysteine 117 of ADP-ribose glycohydrolase MACROD2

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 123 of ADP-ribose glycohydrolase MACROD2

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-ribose glycohydrolase MACROD2 between cysteines 184 and 222. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4iqy
Structure name
crystal structure of the human protein-proximal adp-ribosyl-hydrolase macrod2
Structure deposition date
2013-01-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
100
Peptide accession
A1Z1Q3
Residue number A
184
Residue number B
222
Peptide name
ADP-ribose glycohydrolase MACROD2

Ligandability

Cysteine 184 of ADP-ribose glycohydrolase MACROD2

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 222 of ADP-ribose glycohydrolase MACROD2

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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