a tool for identifying drug-targetable redox-active disulphides

E3 ubiquitin-protein ligase RNF25

Intramolecular

Cysteine 153 and cysteine 201

Cysteine 153 and cysteine 198

Cysteine 198 and cysteine 201

Cysteine 135 and cysteine 138

Cysteine 138 and cysteine 161

Cysteine 135 and cysteine 161

Cysteine 135 and cysteine 159

Cysteine 159 and cysteine 161

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF25 between cysteines 153 and 201.

Details

Redox score ?

86

PDB code

Structure name

crystal structure of ubch5b in complex with the ring-u5br fragment of ao7 (y165a)

Structure deposition date

2013-10-08

Thiol separation (Å)

4

Half-sphere exposure sum ?

36

Minimum pK_a ?

7

% buried

0

Peptide accession

Residue number A

153

Residue number B

201

Peptide name

E3 ubiquitin-protein ligase RNF25

Ligandability

Cysteine 153 of E3 ubiquitin-protein ligase RNF25

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 201 of E3 ubiquitin-protein ligase RNF25

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 E3 ubiquitin-protein ligase RNF25 between cysteines 153 and 198.

Details

Redox score ?

81

PDB code

Structure name

crystal structure of ubch5b in complex with the ring-u5br fragment of ao7

Structure deposition date

2013-10-08

Thiol separation (Å)

4

Half-sphere exposure sum ?

48

Minimum pK_a ?

8

% buried

24

Peptide accession

Residue number A

153

Residue number B

198

Peptide name

E3 ubiquitin-protein ligase RNF25

Ligandability

Cysteine 153 of E3 ubiquitin-protein ligase RNF25

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 198 of E3 ubiquitin-protein ligase RNF25

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 E3 ubiquitin-protein ligase RNF25 between cysteines 198 and 201.

Details

Redox score ?

77

PDB code

Structure name

crystal structure of ubch5b in complex with the ring-u5br fragment of ao7

Structure deposition date

2013-10-08

Thiol separation (Å)

4

Half-sphere exposure sum ?

51

Minimum pK_a ?

8

% buried

20

Peptide accession

Residue number A

198

Residue number B

201

Peptide name

E3 ubiquitin-protein ligase RNF25

Ligandability

Cysteine 198 of E3 ubiquitin-protein ligase RNF25

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 201 of E3 ubiquitin-protein ligase RNF25

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 E3 ubiquitin-protein ligase RNF25 between cysteines 135 and 138.

Details

Redox score ?

77

PDB code

Structure name

crystal structure of ubch5b in complex with the ring-u5br fragment of ao7

Structure deposition date

2013-10-08

Thiol separation (Å)

4

Half-sphere exposure sum ?

72

Minimum pK_a ?

7

% buried

nan

Peptide accession

Residue number A

135

Residue number B

138

Peptide name

E3 ubiquitin-protein ligase RNF25

Ligandability

Cysteine 135 of E3 ubiquitin-protein ligase RNF25

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 138 of E3 ubiquitin-protein ligase RNF25

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 E3 ubiquitin-protein ligase RNF25 between cysteines 138 and 161.

Details

Redox score ?

72

PDB code

Structure name

crystal structure of ubch5b in complex with the ring-u5br fragment of ao7

Structure deposition date

2013-10-08

Thiol separation (Å)

4

Half-sphere exposure sum ?

79

Minimum pK_a ?

7

% buried

84

Peptide accession

Residue number A

138

Residue number B

161

Peptide name

E3 ubiquitin-protein ligase RNF25

Ligandability

Cysteine 138 of E3 ubiquitin-protein ligase RNF25

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 161 of E3 ubiquitin-protein ligase RNF25

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 E3 ubiquitin-protein ligase RNF25 between cysteines 135 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

50

PDB code

Structure name

crystal structure of ubch5b in complex with the ring-u5br fragment of ao7

Structure deposition date

2013-10-08

Thiol separation (Å)

4

Half-sphere exposure sum ?

73

Minimum pK_a ?

19

% buried

nan

Peptide accession

Residue number A

135

Residue number B

161

Peptide name

E3 ubiquitin-protein ligase RNF25

Ligandability

Cysteine 135 of E3 ubiquitin-protein ligase RNF25

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 161 of E3 ubiquitin-protein ligase RNF25

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 E3 ubiquitin-protein ligase RNF25 between cysteines 135 and 159. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

37

PDB code

Structure name

crystal structure of ubch5b in complex with the ring-u5br fragment of ao7 (y165a)

Structure deposition date

2013-10-08

Thiol separation (Å)

10

Half-sphere exposure sum ?

63

Minimum pK_a ?

10

% buried

nan

Peptide accession

Residue number A

135

Residue number B

159

Peptide name

E3 ubiquitin-protein ligase RNF25

Ligandability

Cysteine 135 of E3 ubiquitin-protein ligase RNF25

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 159 of E3 ubiquitin-protein ligase RNF25

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 E3 ubiquitin-protein ligase RNF25 between cysteines 159 and 161. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

37

PDB code

Structure name

crystal structure of ubch5b in complex with the ring-u5br fragment of ao7 (p199a)

Structure deposition date

2013-10-08

Thiol separation (Å)

9

Half-sphere exposure sum ?

69

Minimum pK_a ?

10

% buried

59

Peptide accession

Residue number A

159

Residue number B

161

Peptide name

E3 ubiquitin-protein ligase RNF25

Ligandability

Cysteine 159 of E3 ubiquitin-protein ligase RNF25

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 161 of E3 ubiquitin-protein ligase RNF25

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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