a tool for identifying drug-targetable redox-active disulphides

Insulin-like growth factor 2 mRNA-binding protein 1

Intramolecular

Cysteine 257 and cysteine 337

Cysteine 336 and cysteine 337

Cysteine 257 and cysteine 336

Cysteine 253 and cysteine 257

A redox-regulated disulphide may form within Insulin-like growth factor 2 mRNA-binding protein 1 between cysteines 257 and 337.

Details

Redox score ?

68

PDB code

Structure name

imp1 kh1 and kh2 domains create a structural platform with unique rna recognition and re-modelling properties

Structure deposition date

2019-01-09

Thiol separation (Å)

4

Half-sphere exposure sum ?

82

Minimum pK_a ?

8

% buried

80

Peptide accession

Residue number A

257

Residue number B

337

Peptide name

Insulin-like growth factor 2 mRNA-binding protein 1

Ligandability

Cysteine 257 of Insulin-like growth factor 2 mRNA-binding protein 1

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 337 of Insulin-like growth factor 2 mRNA-binding protein 1

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 Insulin-like growth factor 2 mRNA-binding protein 1 between cysteines 336 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

57

PDB code

Structure name

imp1 kh1 and kh2 domains create a structural platform with unique rna recognition and re-modelling properties

Structure deposition date

2019-01-09

Thiol separation (Å)

7

Half-sphere exposure sum ?

75

Minimum pK_a ?

8

% buried

55

Peptide accession

Residue number A

336

Residue number B

337

Peptide name

Insulin-like growth factor 2 mRNA-binding protein 1

Ligandability

Cysteine 336 of Insulin-like growth factor 2 mRNA-binding protein 1

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 337 of Insulin-like growth factor 2 mRNA-binding protein 1

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 Insulin-like growth factor 2 mRNA-binding protein 1 between cysteines 257 and 336. 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

imp1 kh1 and kh2 domains create a structural platform with unique rna recognition and re-modelling properties

Structure deposition date

2019-01-09

Thiol separation (Å)

8

Half-sphere exposure sum ?

82

Minimum pK_a ?

11

% buried

76

Peptide accession

Residue number A

257

Residue number B

336

Peptide name

Insulin-like growth factor 2 mRNA-binding protein 1

Ligandability

Cysteine 257 of Insulin-like growth factor 2 mRNA-binding protein 1

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 336 of Insulin-like growth factor 2 mRNA-binding protein 1

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 Insulin-like growth factor 2 mRNA-binding protein 1 between cysteines 253 and 257. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

38

PDB code

Structure name

imp1 kh1 and kh2 domains create a structural platform with unique rna recognition and re-modelling properties

Structure deposition date

2019-01-09

Thiol separation (Å)

9

Half-sphere exposure sum ?

83

Minimum pK_a ?

10

% buried

80

Peptide accession

Residue number A

253

Residue number B

257

Peptide name

Insulin-like growth factor 2 mRNA-binding protein 1

Ligandability

Cysteine 253 of Insulin-like growth factor 2 mRNA-binding protein 1

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 257 of Insulin-like growth factor 2 mRNA-binding protein 1

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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