a tool for identifying drug-targetable redox-active disulphides

Glomulin

Intramolecular

Cysteine 174 and cysteine 177 L

Cysteine 72 and cysteine 75

Cysteine 176 and cysteine 177 L

Cysteine 174 and cysteine 176 L

Cysteine 177 and cysteine 218 L

A redox-regulated disulphide may form within Glomulin between cysteines 174 and 177. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

52

PDB code

Structure name

structure of a glomulin-rbx1-cul1 complex

Structure deposition date

2012-05-11

Thiol separation (Å)

6

Half-sphere exposure sum ?

74

Minimum pK_a ?

11

% buried

70

Peptide accession

Residue number A

174

Residue number B

177

Peptide name

Glomulin

Ligandability

Cysteine 174 of Glomulin

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 177 of Glomulin

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Glomulin between cysteines 72 and 75. 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

structure of a glomulin-rbx1-cul1 complex

Structure deposition date

2012-05-11

Thiol separation (Å)

9

Half-sphere exposure sum ?

nan

Minimum pK_a ?

9

% buried

8

Peptide accession

Residue number A

72

Residue number B

75

Peptide name

Glomulin

Ligandability

Cysteine 72 of Glomulin

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 75 of Glomulin

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 Glomulin between cysteines 176 and 177. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

45

PDB code

Structure name

structure of a glomulin-rbx1-cul1 complex

Structure deposition date

2012-05-11

Thiol separation (Å)

7

Half-sphere exposure sum ?

76

Minimum pK_a ?

12

% buried

86

Peptide accession

Residue number A

176

Residue number B

177

Peptide name

Glomulin

Ligandability

Cysteine 176 of Glomulin

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 177 of Glomulin

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Glomulin between cysteines 174 and 176. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

39

PDB code

Structure name

structure of a glomulin-rbx1-cul1 complex

Structure deposition date

2012-05-11

Thiol separation (Å)

9

Half-sphere exposure sum ?

73

Minimum pK_a ?

11

% buried

59

Peptide accession

Residue number A

174

Residue number B

176

Peptide name

Glomulin

Ligandability

Cysteine 174 of Glomulin

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 176 of Glomulin

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Glomulin between cysteines 177 and 218. 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

structure of a glomulin-rbx1-cul1 complex

Structure deposition date

2012-05-11

Thiol separation (Å)

9

Half-sphere exposure sum ?

73

Minimum pK_a ?

11

% buried

96

Peptide accession

Residue number A

177

Residue number B

218

Peptide name

Glomulin

Ligandability

Cysteine 177 of Glomulin

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 218 of Glomulin

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.

Ligandable in the dataset of Kuljanin et al.

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