a tool for identifying drug-targetable redox-active disulphides

Protein ELYS

Intramolecular

Cysteine 171 and cysteine 177

Cysteine 282 and cysteine 283

Cysteine 283 and cysteine 327

Cysteine 481 and cysteine 492

A redox-regulated disulphide may form within Protein ELYS between cysteines 171 and 177. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

49

PDB code

Structure name

nucleoporin elys (aa1-494), mus musculus

Structure deposition date

2012-11-17

Thiol separation (Å)

8

Half-sphere exposure sum ?

59

Minimum pK_a ?

10

% buried

61

Peptide accession

Residue number A

171

Residue number B

177

Peptide name

Protein ELYS

Ligandability

Cysteine 171 of Protein ELYS

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 177 of Protein ELYS

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 Protein ELYS between cysteines 282 and 283. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

40

PDB code

Structure name

nucleoporin elys (aa1-494), mus musculus

Structure deposition date

2012-11-17

Thiol separation (Å)

7

Half-sphere exposure sum ?

79

Minimum pK_a ?

12

% buried

76

Peptide accession

Residue number A

282

Residue number B

283

Peptide name

Protein ELYS

Ligandability

Cysteine 282 of Protein ELYS

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 283 of Protein ELYS

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 Protein ELYS between cysteines 283 and 327. 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

nucleoporin elys (aa1-494), mus musculus

Structure deposition date

2012-11-17

Thiol separation (Å)

9

Half-sphere exposure sum ?

70

Minimum pK_a ?

12

% buried

96

Peptide accession

Residue number A

283

Residue number B

327

Peptide name

Protein ELYS

Ligandability

Cysteine 283 of Protein ELYS

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 327 of Protein ELYS

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 Protein ELYS between cysteines 481 and 492. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

32

PDB code

Structure name

nucleoporin elys (aa1-494), mus musculus

Structure deposition date

2012-11-17

Thiol separation (Å)

9

Half-sphere exposure sum ?

87

Minimum pK_a ?

12

% buried

92

Peptide accession

Residue number A

481

Residue number B

492

Peptide name

Protein ELYS

Ligandability

Cysteine 481 of Protein ELYS

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 492 of Protein ELYS

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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