ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Double-stranded RNA-specific editase 1

Intramolecular
Cysteine 451 and cysteine 556
Cysteine 377 and cysteine 451
Cysteine 377 and cysteine 393
Cysteine 377 and cysteine 556
Cysteine 668 and cysteine 674
A redox-regulated disulphide may form within Double-stranded RNA-specific editase 1 between cysteines 451 and 556 (451 and 516 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
5ed2
Structure name
human adenosine deaminase acting on dsrna (adar2) mutant e488q bound to dsrna sequence derived from human gli1 gene
Structure deposition date
2015-10-20
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
16
% buried
nan
Peptide accession
P78563
Residue number A
451
Residue number B
556
Peptide name
Double-stranded RNA-specific editase 1

Ligandability

Cysteine 451 of Double-stranded RNA-specific editase 1

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 556 of Double-stranded RNA-specific editase 1

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 Double-stranded RNA-specific editase 1 between cysteines 377 and 451. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
8e4x
Structure name
human adenosine deaminase acting on dsrna (adar2-r2d) bound to dsrna containing a g:3-deaza da pair adjacent to the target site
Structure deposition date
2022-08-19
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
4
% buried
100
Peptide accession
P78563
Residue number A
377
Residue number B
451
Peptide name
Double-stranded RNA-specific editase 1

Ligandability

Cysteine 377 of Double-stranded RNA-specific editase 1

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 451 of Double-stranded RNA-specific editase 1

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 Double-stranded RNA-specific editase 1 between cysteines 377 and 393. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5ed1
Structure name
human adenosine deaminase acting on dsrna (adar2) mutant e488q bound to dsrna sequence derived from s
Structure deposition date
2015-10-20
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
100
Peptide accession
P78563
Residue number A
377
Residue number B
393
Peptide name
Double-stranded RNA-specific editase 1

Ligandability

Cysteine 377 of Double-stranded RNA-specific editase 1

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 393 of Double-stranded RNA-specific editase 1

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 Double-stranded RNA-specific editase 1 between cysteines 377 and 556 (377 and 516 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6vff
Structure name
dimer of human adenosine deaminase acting on dsrna (adar2) mutant e488q bound to dsrna sequence derived from human gli1 gene
Structure deposition date
2020-01-03
Thiol separation (Å)
7
Half-sphere exposure sum ?
86
Minimum pKa ?
12
% buried
100
Peptide accession
P78563
Residue number A
377
Residue number B
556
Peptide name
Double-stranded RNA-specific editase 1

Ligandability

Cysteine 377 of Double-stranded RNA-specific editase 1

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 556 of Double-stranded RNA-specific editase 1

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 Double-stranded RNA-specific editase 1 between cysteines 668 and 674 (628 and 634 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
5ed2
Structure name
human adenosine deaminase acting on dsrna (adar2) mutant e488q bound to dsrna sequence derived from human gli1 gene
Structure deposition date
2015-10-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
56
Peptide accession
P78563
Residue number A
668
Residue number B
674
Peptide name
Double-stranded RNA-specific editase 1

Ligandability

Cysteine 668 of Double-stranded RNA-specific editase 1

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 674 of Double-stranded RNA-specific editase 1

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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