ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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ATP-dependent RNA helicase DHX15

Intramolecular
Cysteine 599 and cysteine 644
Cysteine 579 and cysteine 583
Cysteine 174 and cysteine 190
A redox-regulated disulphide may form within ATP-dependent RNA helicase DHX15 between cysteines 599 and 644. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5xdr
Structure name
crystal structure of human deah-box rna helicase dhx15 in complex with adp
Structure deposition date
2017-03-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
11
% buried
69
Peptide accession
O43143
Residue number A
599
Residue number B
644
Peptide name
ATP-dependent RNA helicase DHX15

Ligandability

Cysteine 599 of ATP-dependent RNA helicase DHX15

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 644 of ATP-dependent RNA helicase DHX15

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 DHX15 between cysteines 579 and 583. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
5xdr
Structure name
crystal structure of human deah-box rna helicase dhx15 in complex with adp
Structure deposition date
2017-03-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
66
Peptide accession
O43143
Residue number A
579
Residue number B
583
Peptide name
ATP-dependent RNA helicase DHX15

Ligandability

Cysteine 579 of ATP-dependent RNA helicase DHX15

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 583 of ATP-dependent RNA helicase DHX15

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 DHX15 between cysteines 174 and 190. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
8ejm
Structure name
crystal structure of human deah-box helicase dhx15 in complex with sugp1 g-patch
Structure deposition date
2022-09-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
O43143
Residue number A
174
Residue number B
190
Peptide name
ATP-dependent RNA helicase DHX15

Ligandability

Cysteine 174 of ATP-dependent RNA helicase DHX15

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 190 of ATP-dependent RNA helicase DHX15

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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