ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Decapping and exoribonuclease protein

Intramolecular
Cysteine 196 and cysteine 237
Cysteine 244 and cysteine 250
Cysteine 51 and cysteine 217
Cysteine 237 and cysteine 250
Cysteine 327 and cysteine 331
A redox-regulated disulphide may form within Decapping and exoribonuclease protein between cysteines 196 and 237.

Details

Redox score ?
68
PDB code
6wre
Structure name
crystal structure of mouse dxo in complex with 5'-oh rna substrate mimic and calcium ion
Structure deposition date
2020-04-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
8
% buried
100
Peptide accession
O70348
Residue number A
196
Residue number B
237
Peptide name
Decapping and exoribonuclease protein

Ligandability

Cysteine 196 of Decapping and exoribonuclease protein

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 237 of Decapping and exoribonuclease protein

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 Decapping and exoribonuclease protein between cysteines 244 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
6wre
Structure name
crystal structure of mouse dxo in complex with 5'-oh rna substrate mimic and calcium ion
Structure deposition date
2020-04-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
20
Peptide accession
O70348
Residue number A
244
Residue number B
250
Peptide name
Decapping and exoribonuclease protein

Ligandability

Cysteine 244 of Decapping and exoribonuclease protein

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 250 of Decapping and exoribonuclease protein

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 Decapping and exoribonuclease protein between cysteines 51 and 217. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
3fqj
Structure name
crystal structure of the mouse dom3z in complex with gdp
Structure deposition date
2009-01-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
80
Peptide accession
O70348
Residue number A
51
Residue number B
217
Peptide name
Decapping and exoribonuclease protein

Ligandability

Cysteine 51 of Decapping and exoribonuclease protein

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 217 of Decapping and exoribonuclease protein

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 Decapping and exoribonuclease protein between cysteines 237 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6wre
Structure name
crystal structure of mouse dxo in complex with 5'-oh rna substrate mimic and calcium ion
Structure deposition date
2020-04-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
70
Peptide accession
O70348
Residue number A
237
Residue number B
250
Peptide name
Decapping and exoribonuclease protein

Ligandability

Cysteine 237 of Decapping and exoribonuclease protein

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 250 of Decapping and exoribonuclease protein

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 Decapping and exoribonuclease protein between cysteines 327 and 331. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
3fqj
Structure name
crystal structure of the mouse dom3z in complex with gdp
Structure deposition date
2009-01-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
O70348
Residue number A
327
Residue number B
331
Peptide name
Decapping and exoribonuclease protein

Ligandability

Cysteine 327 of Decapping and exoribonuclease protein

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 331 of Decapping and exoribonuclease protein

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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