a tool for identifying drug-targetable redox-active disulphides

Zinc finger protein 57

Intramolecular

Cysteine 170 and cysteine 173

Cysteine 142 and cysteine 145

Cysteine 170 and cysteine 176

Cysteine 173 and cysteine 176

A redox-regulated disulphide may form within Zinc finger protein 57 between cysteines 170 and 173.

Details

Redox score ?

88

PDB code

Structure name

zfp57 mutant (e182q) in complex with 5-carboxylcytosine dna

Structure deposition date

2013-08-15

Thiol separation (Å)

4

Half-sphere exposure sum ?

39

Minimum pK_a ?

6

% buried

0

Peptide accession

Residue number A

170

Residue number B

173

Peptide name

Zinc finger protein 57

Ligandability

Cysteine 170 of Zinc finger protein 57

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 173 of Zinc finger protein 57

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 Zinc finger protein 57 between cysteines 142 and 145.

Details

Redox score ?

81

PDB code

Structure name

zfp57 mutant (e182q) in complex with 5-carboxylcytosine dna

Structure deposition date

2013-08-15

Thiol separation (Å)

4

Half-sphere exposure sum ?

41

Minimum pK_a ?

8

% buried

25

Peptide accession

Residue number A

142

Residue number B

145

Peptide name

Zinc finger protein 57

Ligandability

Cysteine 142 of Zinc finger protein 57

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 145 of Zinc finger protein 57

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 Zinc finger protein 57 between cysteines 170 and 176. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

53

PDB code

Structure name

zfp57 mutant (e182q) in complex with 5-carboxylcytosine dna

Structure deposition date

2013-08-15

Thiol separation (Å)

10

Half-sphere exposure sum ?

47

Minimum pK_a ?

6

% buried

10

Peptide accession

Residue number A

170

Residue number B

176

Peptide name

Zinc finger protein 57

Ligandability

Cysteine 170 of Zinc finger protein 57

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 176 of Zinc finger protein 57

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 Zinc finger protein 57 between cysteines 173 and 176. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

51

PDB code

Structure name

zfp57 mutant (e182q) in complex with 5-carboxylcytosine dna

Structure deposition date

2013-08-15

Thiol separation (Å)

9

Half-sphere exposure sum ?

38

Minimum pK_a ?

8

% buried

10

Peptide accession

Residue number A

173

Residue number B

176

Peptide name

Zinc finger protein 57

Ligandability

Cysteine 173 of Zinc finger protein 57

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 176 of Zinc finger protein 57

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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