ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Exosome complex component RRP46

Intermolecular
Cysteine 138 and cysteine 83 of Exosome complex component RRP40
Intramolecular
Cysteine 157 and cysteine 209
Cysteine 132 and cysteine 133
Cysteine 102 and cysteine 138
Cysteine 33 and cysteine 132
Cysteine 138 and cysteine 153
Cysteine 33 and cysteine 138
A redox-regulated disulphide may form between cysteine 138 of Exosome complex component RRP46 and cysteine 83 of Exosome complex component RRP40. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
6d6r
Structure name
human nuclear exosome-mtr4 rna complex - composite map after focused reconstruction
Structure deposition date
2018-04-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
99
Minimum pKa ?
11
% buried
100
Peptide A name
Exosome complex component RRP46
Peptide B name
Exosome complex component RRP40
Peptide A accession
Q9NQT4
Peptide B accession
Q9NQT5
Peptide A residue number
138
Peptide B residue number
83

Ligandability

Cysteine 138 of Exosome complex component RRP46

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 83 of Exosome complex component RRP40

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 Exosome complex component RRP46 between cysteines 157 and 209. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2nn6
Structure name
structure of the human rna exosome composed of rrp41, rrp45, rrp46, rrp43, mtr3, rrp42, csl4, rrp4, and rrp40
Structure deposition date
2006-10-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
87
Minimum pKa ?
12
% buried
100
Peptide accession
Q9NQT4
Residue number A
157
Residue number B
209
Peptide name
Exosome complex component RRP46

Ligandability

Cysteine 157 of Exosome complex component RRP46

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 209 of Exosome complex component RRP46

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 Exosome complex component RRP46 between cysteines 132 and 133. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2nn6
Structure name
structure of the human rna exosome composed of rrp41, rrp45, rrp46, rrp43, mtr3, rrp42, csl4, rrp4, and rrp40
Structure deposition date
2006-10-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
104
Minimum pKa ?
12
% buried
100
Peptide accession
Q9NQT4
Residue number A
132
Residue number B
133
Peptide name
Exosome complex component RRP46

Ligandability

Cysteine 132 of Exosome complex component RRP46

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 133 of Exosome complex component RRP46

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 Exosome complex component RRP46 between cysteines 102 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
2nn6
Structure name
structure of the human rna exosome composed of rrp41, rrp45, rrp46, rrp43, mtr3, rrp42, csl4, rrp4, and rrp40
Structure deposition date
2006-10-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
105
Minimum pKa ?
12
% buried
100
Peptide accession
Q9NQT4
Residue number A
102
Residue number B
138
Peptide name
Exosome complex component RRP46

Ligandability

Cysteine 102 of Exosome complex component RRP46

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 Exosome complex component RRP46

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 Exosome complex component RRP46 between cysteines 33 and 132. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2nn6
Structure name
structure of the human rna exosome composed of rrp41, rrp45, rrp46, rrp43, mtr3, rrp42, csl4, rrp4, and rrp40
Structure deposition date
2006-10-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
100
Minimum pKa ?
12
% buried
100
Peptide accession
Q9NQT4
Residue number A
33
Residue number B
132
Peptide name
Exosome complex component RRP46

Ligandability

Cysteine 33 of Exosome complex component RRP46

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 Exosome complex component RRP46

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 Exosome complex component RRP46 between cysteines 138 and 153. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
2nn6
Structure name
structure of the human rna exosome composed of rrp41, rrp45, rrp46, rrp43, mtr3, rrp42, csl4, rrp4, and rrp40
Structure deposition date
2006-10-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
104
Minimum pKa ?
12
% buried
100
Peptide accession
Q9NQT4
Residue number A
138
Residue number B
153
Peptide name
Exosome complex component RRP46

Ligandability

Cysteine 138 of Exosome complex component RRP46

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 153 of Exosome complex component RRP46

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 Exosome complex component RRP46 between cysteines 33 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
2nn6
Structure name
structure of the human rna exosome composed of rrp41, rrp45, rrp46, rrp43, mtr3, rrp42, csl4, rrp4, and rrp40
Structure deposition date
2006-10-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
104
Minimum pKa ?
12
% buried
100
Peptide accession
Q9NQT4
Residue number A
33
Residue number B
138
Peptide name
Exosome complex component RRP46

Ligandability

Cysteine 33 of Exosome complex component RRP46

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 Exosome complex component RRP46

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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