a tool for identifying drug-targetable redox-active disulphides

E3 ubiquitin-protein ligase RNF113A

Intramolecular

Cysteine 202 and cysteine 217

Cysteine 262 and cysteine 265

Cysteine 262 and cysteine 282

Cysteine 265 and cysteine 285

Cysteine 262 and cysteine 285

Cysteine 265 and cysteine 282

Cysteine 211 and cysteine 217

Cysteine 277 and cysteine 299

Cysteine 296 and cysteine 299

Cysteine 277 and cysteine 296

Cysteine 282 and cysteine 285

Cysteine 202 and cysteine 211

A redox-regulated disulphide may form within E3 ubiquitin-protein ligase RNF113A between cysteines 202 and 217.

Details

Redox score ?

90

PDB code

Structure name

human bact spliceosome core structure

Structure deposition date

2018-01-03

Thiol separation (Å)

4

Half-sphere exposure sum ?

67

Minimum pK_a ?

2

% buried

92

Peptide accession

Residue number A

202

Residue number B

217

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 202 of E3 ubiquitin-protein ligase RNF113A

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 217 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 262 and 265.

Details

Redox score ?

87

PDB code

Structure name

cryo-em structure of the activated human minor spliceosome (minor bact complex)

Structure deposition date

2021-01-14

Thiol separation (Å)

4

Half-sphere exposure sum ?

nan

Minimum pK_a ?

7

% buried

2

Peptide accession

Residue number A

262

Residue number B

265

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 262 of E3 ubiquitin-protein ligase RNF113A

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 265 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 262 and 282.

Details

Redox score ?

84

PDB code

Structure name

human bact spliceosome core structure

Structure deposition date

2018-01-03

Thiol separation (Å)

4

Half-sphere exposure sum ?

nan

Minimum pK_a ?

6

% buried

1

Peptide accession

Residue number A

262

Residue number B

282

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 262 of E3 ubiquitin-protein ligase RNF113A

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 282 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 265 and 285.

Details

Redox score ?

79

PDB code

Structure name

human bact spliceosome core structure

Structure deposition date

2018-01-03

Thiol separation (Å)

4

Half-sphere exposure sum ?

44

Minimum pK_a ?

9

% buried

0

Peptide accession

Residue number A

265

Residue number B

285

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 265 of E3 ubiquitin-protein ligase RNF113A

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 285 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 262 and 285.

Details

Redox score ?

75

PDB code

Structure name

human bact spliceosome core structure

Structure deposition date

2018-01-03

Thiol separation (Å)

6

Half-sphere exposure sum ?

nan

Minimum pK_a ?

6

% buried

1

Peptide accession

Residue number A

262

Residue number B

285

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 262 of E3 ubiquitin-protein ligase RNF113A

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 285 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 265 and 282.

Details

Redox score ?

74

PDB code

Structure name

cryo-em structure of the activated human minor spliceosome (minor bact complex)

Structure deposition date

2021-01-14

Thiol separation (Å)

5

Half-sphere exposure sum ?

46

Minimum pK_a ?

9

% buried

0

Peptide accession

Residue number A

265

Residue number B

282

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 265 of E3 ubiquitin-protein ligase RNF113A

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 282 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 211 and 217.

Details

Redox score ?

73

PDB code

Structure name

cryo-em structure of the activated human minor spliceosome (minor bact complex)

Structure deposition date

2021-01-14

Thiol separation (Å)

4

Half-sphere exposure sum ?

65

Minimum pK_a ?

10

% buried

nan

Peptide accession

Residue number A

211

Residue number B

217

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 211 of E3 ubiquitin-protein ligase RNF113A

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 217 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 277 and 299.

Details

Redox score ?

71

PDB code

Structure name

human bact spliceosome core structure

Structure deposition date

2018-01-03

Thiol separation (Å)

5

Half-sphere exposure sum ?

33

Minimum pK_a ?

9

% buried

10

Peptide accession

Residue number A

277

Residue number B

299

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 277 of E3 ubiquitin-protein ligase RNF113A

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 299 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 296 and 299.

Details

Redox score ?

68

PDB code

Structure name

human bact spliceosome core structure

Structure deposition date

2018-01-03

Thiol separation (Å)

6

Half-sphere exposure sum ?

42

Minimum pK_a ?

9

% buried

12

Peptide accession

Residue number A

296

Residue number B

299

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 296 of E3 ubiquitin-protein ligase RNF113A

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 299 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 277 and 296.

Details

Redox score ?

67

PDB code

Structure name

human bact spliceosome core structure

Structure deposition date

2018-01-03

Thiol separation (Å)

6

Half-sphere exposure sum ?

53

Minimum pK_a ?

9

% buried

21

Peptide accession

Residue number A

277

Residue number B

296

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 277 of E3 ubiquitin-protein ligase RNF113A

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 296 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 282 and 285.

Details

Redox score ?

65

PDB code

Structure name

human bact spliceosome core structure

Structure deposition date

2018-01-03

Thiol separation (Å)

5

Half-sphere exposure sum ?

54

Minimum pK_a ?

10

% buried

0

Peptide accession

Residue number A

282

Residue number B

285

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 282 of E3 ubiquitin-protein ligase RNF113A

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 285 of E3 ubiquitin-protein ligase RNF113A

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 RNF113A between cysteines 202 and 211. 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

cryo-em structure of the activated human minor spliceosome (minor bact complex)

Structure deposition date

2021-01-14

Thiol separation (Å)

4

Half-sphere exposure sum ?

64

Minimum pK_a ?

19

% buried

nan

Peptide accession

Residue number A

202

Residue number B

211

Peptide name

E3 ubiquitin-protein ligase RNF113A

Ligandability

Cysteine 202 of E3 ubiquitin-protein ligase RNF113A

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 211 of E3 ubiquitin-protein ligase RNF113A

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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