ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Probable ATP-dependent RNA helicase DDX6

Intramolecular
Cysteine 361 and cysteine 385
Cysteine 341 and cysteine 361
Cysteine 341 and cysteine 390
A redox-regulated disulphide may form within Probable ATP-dependent RNA helicase DDX6 between cysteines 361 and 385 (350 and 374 respectively in this structure).

Details

Redox score ?
63
PDB code
6s8s
Structure name
extended structure of the human ddx6 c-terminal domain in complex with an edc3 fdf peptide
Structure deposition date
2019-07-10
Thiol separation (Å)
6
Half-sphere exposure sum ?
59
Minimum pKa ?
9
% buried
56
Peptide accession
P26196
Residue number A
361
Residue number B
385
Peptide name
Probable ATP-dependent RNA helicase DDX6

Ligandability

Cysteine 361 of Probable ATP-dependent RNA helicase DDX6

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 385 of Probable ATP-dependent RNA helicase DDX6

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 Probable ATP-dependent RNA helicase DDX6 between cysteines 341 and 361. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6f9s
Structure name
crystal structure of the c-terminal reca domain of ddx6 in complex with a conserved peptide from lsm14
Structure deposition date
2017-12-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
92
Peptide accession
P26196
Residue number A
341
Residue number B
361
Peptide name
Probable ATP-dependent RNA helicase DDX6

Ligandability

Cysteine 341 of Probable ATP-dependent RNA helicase DDX6

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 361 of Probable ATP-dependent RNA helicase DDX6

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 Probable ATP-dependent RNA helicase DDX6 between cysteines 341 and 390 (330 and 379 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
6s8s
Structure name
extended structure of the human ddx6 c-terminal domain in complex with an edc3 fdf peptide
Structure deposition date
2019-07-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
100
Peptide accession
P26196
Residue number A
341
Residue number B
390
Peptide name
Probable ATP-dependent RNA helicase DDX6

Ligandability

Cysteine 341 of Probable ATP-dependent RNA helicase DDX6

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 390 of Probable ATP-dependent RNA helicase DDX6

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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