a tool for identifying drug-targetable redox-active disulphides

Probable ATP-dependent RNA helicase DDX5

Intramolecular

Cysteine 191 and cysteine 194

Cysteine 170 and cysteine 191

Cysteine 200 and cysteine 221 L

Cysteine 170 and cysteine 221

A redox-regulated disulphide may form within Probable ATP-dependent RNA helicase DDX5 between cysteines 191 and 194. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

45

PDB code

Structure name

human dead-box rna helicase ddx5 (p68), conserved domain i in complex with adp

Structure deposition date

2008-11-27

Thiol separation (Å)

7

Half-sphere exposure sum ?

71

Minimum pK_a ?

11

% buried

96

Peptide accession

Residue number A

191

Residue number B

194

Peptide name

Probable ATP-dependent RNA helicase DDX5

Ligandability

Cysteine 191 of Probable ATP-dependent RNA helicase DDX5

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 194 of Probable ATP-dependent RNA helicase DDX5

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 DDX5 between cysteines 170 and 191. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

35

PDB code

Structure name

human dead-box rna helicase ddx5 (p68), conserved domain i in complex with adp

Structure deposition date

2008-11-27

Thiol separation (Å)

9

Half-sphere exposure sum ?

76

Minimum pK_a ?

11

% buried

94

Peptide accession

Residue number A

170

Residue number B

191

Peptide name

Probable ATP-dependent RNA helicase DDX5

Ligandability

Cysteine 170 of Probable ATP-dependent RNA helicase DDX5

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 191 of Probable ATP-dependent RNA helicase DDX5

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 DDX5 between cysteines 200 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

34

PDB code

Structure name

human dead-box rna helicase ddx5 (p68), conserved domain i in complex with adp

Structure deposition date

2008-11-27

Thiol separation (Å)

8

Half-sphere exposure sum ?

91

Minimum pK_a ?

12

% buried

80

Peptide accession

Residue number A

200

Residue number B

221

Peptide name

Probable ATP-dependent RNA helicase DDX5

Ligandability

Cysteine 200 of Probable ATP-dependent RNA helicase DDX5

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 221 of Probable ATP-dependent RNA helicase DDX5

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 DDX5 between cysteines 170 and 221. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

29

PDB code

Structure name

human dead-box rna helicase ddx5 (p68), conserved domain i in complex with adp

Structure deposition date

2008-11-27

Thiol separation (Å)

9

Half-sphere exposure sum ?

92

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

170

Residue number B

221

Peptide name

Probable ATP-dependent RNA helicase DDX5

Ligandability

Cysteine 170 of Probable ATP-dependent RNA helicase DDX5

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 221 of Probable ATP-dependent RNA helicase DDX5

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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