a tool for identifying drug-targetable redox-active disulphides

Zinc transporter ZIP4

Intramolecular

Cysteine 59 and cysteine 64

Cysteine 266 and cysteine 305

Cysteine 153 and cysteine 188

Cysteine 67 and cysteine 103

Cysteine 64 and cysteine 103

Cysteine 64 and cysteine 67

Cysteine 59 and cysteine 103

Cysteine 59 and cysteine 67

A redox-regulated disulphide may form within Zinc transporter ZIP4 between cysteines 59 and 64.

Details

Redox score ?

90

PDB code

Structure name

crystal structure of the extracellular domain of zip4

Structure deposition date

2014-12-09

Thiol separation (Å)

2

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

59

Residue number B

64

Peptide name

Zinc transporter ZIP4

Ligandability

Cysteine 59 of Zinc transporter ZIP4

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 64 of Zinc transporter ZIP4

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 transporter ZIP4 between cysteines 266 and 305.

Details

Redox score ?

88

PDB code

Structure name

crystal structure of the extracellular domain of zip4

Structure deposition date

2014-12-09

Thiol separation (Å)

2

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

266

Residue number B

305

Peptide name

Zinc transporter ZIP4

Ligandability

Cysteine 266 of Zinc transporter ZIP4

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 305 of Zinc transporter ZIP4

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 transporter ZIP4 between cysteines 153 and 188.

Details

Redox score ?

84

PDB code

Structure name

crystal structure of the extracellular domain of zip4

Structure deposition date

2014-12-09

Thiol separation (Å)

2

Half-sphere exposure sum ?

46

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

153

Residue number B

188

Peptide name

Zinc transporter ZIP4

Ligandability

Cysteine 153 of Zinc transporter ZIP4

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 188 of Zinc transporter ZIP4

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 transporter ZIP4 between cysteines 67 and 103.

Details

Redox score ?

81

PDB code

Structure name

crystal structure of the extracellular domain of zip4

Structure deposition date

2014-12-09

Thiol separation (Å)

2

Half-sphere exposure sum ?

54

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

67

Residue number B

103

Peptide name

Zinc transporter ZIP4

Ligandability

Cysteine 67 of Zinc transporter ZIP4

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 103 of Zinc transporter ZIP4

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 transporter ZIP4 between cysteines 64 and 103.

Details

Redox score ?

63

PDB code

Structure name

crystal structure of the extracellular domain of zip4

Structure deposition date

2014-12-09

Thiol separation (Å)

6

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

64

Residue number B

103

Peptide name

Zinc transporter ZIP4

Ligandability

Cysteine 64 of Zinc transporter ZIP4

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 103 of Zinc transporter ZIP4

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 transporter ZIP4 between cysteines 64 and 67. 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

crystal structure of the extracellular domain of zip4

Structure deposition date

2014-12-09

Thiol separation (Å)

7

Half-sphere exposure sum ?

nan

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

64

Residue number B

67

Peptide name

Zinc transporter ZIP4

Ligandability

Cysteine 64 of Zinc transporter ZIP4

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 67 of Zinc transporter ZIP4

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 transporter ZIP4 between cysteines 59 and 103. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

55

PDB code

Structure name

crystal structure of the extracellular domain of zip4

Structure deposition date

2014-12-09

Thiol separation (Å)

7

Half-sphere exposure sum ?

53

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

59

Residue number B

103

Peptide name

Zinc transporter ZIP4

Ligandability

Cysteine 59 of Zinc transporter ZIP4

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 103 of Zinc transporter ZIP4

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 transporter ZIP4 between cysteines 59 and 67. 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

crystal structure of the extracellular domain of zip4

Structure deposition date

2014-12-09

Thiol separation (Å)

8

Half-sphere exposure sum ?

49

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

59

Residue number B

67

Peptide name

Zinc transporter ZIP4

Ligandability

Cysteine 59 of Zinc transporter ZIP4

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 67 of Zinc transporter ZIP4

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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