ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ATP-dependent RNA helicase DHX58

Intermolecular
Cysteine 559 and cysteine 559
Intramolecular
Cysteine 612 and cysteine 615
Cysteine 559 and cysteine 612
Cysteine 556 and cysteine 615
Cysteine 556 and cysteine 612
Cysteine 556 and cysteine 559
Cysteine 559 and cysteine 615
A redox-regulated disulphide may form between two units of ATP-dependent RNA helicase DHX58 at cysteines 559 and 559. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2w4r
Structure name
crystal structure of the regulatory domain of human lgp2
Structure deposition date
2008-12-01
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
14
% buried
nan
Peptide A name
ATP-dependent RNA helicase DHX58
Peptide B name
ATP-dependent RNA helicase DHX58
Peptide A accession
Q96C10
Peptide B accession
Q96C10
Peptide A residue number
559
Peptide B residue number
559

Ligandability

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 ATP-dependent RNA helicase DHX58 between cysteines 612 and 615.

Details

Redox score ?
77
PDB code
2w4r
Structure name
crystal structure of the regulatory domain of human lgp2
Structure deposition date
2008-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
6
% buried
51
Peptide accession
Q96C10
Residue number A
612
Residue number B
615
Peptide name
ATP-dependent RNA helicase DHX58

Ligandability

Cysteine 612 of ATP-dependent RNA helicase DHX58

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 615 of ATP-dependent RNA helicase DHX58

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 ATP-dependent RNA helicase DHX58 between cysteines 559 and 612.

Details

Redox score ?
76
PDB code
2w4r
Structure name
crystal structure of the regulatory domain of human lgp2
Structure deposition date
2008-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
26
Peptide accession
Q96C10
Residue number A
559
Residue number B
612
Peptide name
ATP-dependent RNA helicase DHX58

Ligandability

Cysteine 559 of ATP-dependent RNA helicase DHX58

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 612 of ATP-dependent RNA helicase DHX58

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 ATP-dependent RNA helicase DHX58 between cysteines 556 and 615.

Details

Redox score ?
75
PDB code
3eqt
Structure name
crystal structure of human lgp2 c-terminal domain in complex with dsrna
Structure deposition date
2008-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
8
% buried
35
Peptide accession
Q96C10
Residue number A
556
Residue number B
615
Peptide name
ATP-dependent RNA helicase DHX58

Ligandability

Cysteine 556 of ATP-dependent RNA helicase DHX58

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 615 of ATP-dependent RNA helicase DHX58

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 ATP-dependent RNA helicase DHX58 between cysteines 556 and 612.

Details

Redox score ?
74
PDB code
2w4r
Structure name
crystal structure of the regulatory domain of human lgp2
Structure deposition date
2008-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
42
Peptide accession
Q96C10
Residue number A
556
Residue number B
612
Peptide name
ATP-dependent RNA helicase DHX58

Ligandability

Cysteine 556 of ATP-dependent RNA helicase DHX58

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 612 of ATP-dependent RNA helicase DHX58

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 ATP-dependent RNA helicase DHX58 between cysteines 556 and 559.

Details

Redox score ?
73
PDB code
3eqt
Structure name
crystal structure of human lgp2 c-terminal domain in complex with dsrna
Structure deposition date
2008-10-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
8
% buried
24
Peptide accession
Q96C10
Residue number A
556
Residue number B
559
Peptide name
ATP-dependent RNA helicase DHX58

Ligandability

Cysteine 556 of ATP-dependent RNA helicase DHX58

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 559 of ATP-dependent RNA helicase DHX58

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 ATP-dependent RNA helicase DHX58 between cysteines 559 and 615.

Details

Redox score ?
60
PDB code
2w4r
Structure name
crystal structure of the regulatory domain of human lgp2
Structure deposition date
2008-12-01
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
14
% buried
54
Peptide accession
Q96C10
Residue number A
559
Residue number B
615
Peptide name
ATP-dependent RNA helicase DHX58

Ligandability

Cysteine 559 of ATP-dependent RNA helicase DHX58

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 615 of ATP-dependent RNA helicase DHX58

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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