a tool for identifying drug-targetable redox-active disulphides

Wilms tumor protein

Intramolecular

Cysteine 385 and cysteine 388

Cysteine 355 and cysteine 360

Cysteine 416 and cysteine 421

Cysteine 325 and cysteine 330

Cysteine 388 and cysteine 416

A redox-regulated disulphide may form within Wilms tumor protein between cysteines 385 and 388.

Details

Redox score ?

92

PDB code

Structure name

structure of the wilms tumor suppressor protein zinc finger domain bound to dna

Structure deposition date

2007-05-04

Thiol separation (Å)

3

Half-sphere exposure sum ?

39

Minimum pK_a ?

6

% buried

0

Peptide accession

Residue number A

385

Residue number B

388

Peptide name

Wilms tumor protein

Ligandability

Cysteine 385 of Wilms tumor protein

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 388 of Wilms tumor protein

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 Wilms tumor protein between cysteines 355 and 360.

Details

Redox score ?

89

PDB code

Structure name

zinc finger domain of wt1(-kts form) with 12+1mer oligonucleotide with 3' triplet ggt

Structure deposition date

2017-09-14

Thiol separation (Å)

4

Half-sphere exposure sum ?

43

Minimum pK_a ?

7

% buried

8

Peptide accession

Residue number A

355

Residue number B

360

Peptide name

Wilms tumor protein

Ligandability

Cysteine 355 of Wilms tumor protein

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 360 of Wilms tumor protein

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 Wilms tumor protein between cysteines 416 and 421 (413 and 418 respectively in this structure).

Details

Redox score ?

88

PDB code

Structure name

wilms tumor protein (wt1) znf2-4 q369h in complex with dna

Structure deposition date

2016-06-23

Thiol separation (Å)

4

Half-sphere exposure sum ?

38

Minimum pK_a ?

7

% buried

0

Peptide accession

Residue number A

416

Residue number B

421

Peptide name

Wilms tumor protein

Ligandability

Cysteine 416 of Wilms tumor protein

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 421 of Wilms tumor protein

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 Wilms tumor protein between cysteines 325 and 330.

Details

Redox score ?

87

PDB code

Structure name

zinc finger domain of wt1(+kts form) with m342r mutation and 17+1mer oligonucleotide with triplet ggt

Structure deposition date

2017-11-11

Thiol separation (Å)

4

Half-sphere exposure sum ?

40

Minimum pK_a ?

8

% buried

0

Peptide accession

Residue number A

325

Residue number B

330

Peptide name

Wilms tumor protein

Ligandability

Cysteine 325 of Wilms tumor protein

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 330 of Wilms tumor protein

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 Wilms tumor protein between cysteines 388 and 416. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

48

PDB code

Structure name

zinc finger domain of wt1(+kts form) with m342r mutation and 17+1mer oligonucleotide with triplet ggt

Structure deposition date

2017-11-11

Thiol separation (Å)

9

Half-sphere exposure sum ?

48

Minimum pK_a ?

10

% buried

nan

Peptide accession

Residue number A

388

Residue number B

416

Peptide name

Wilms tumor protein

Ligandability

Cysteine 388 of Wilms tumor protein

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 416 of Wilms tumor protein

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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