a tool for identifying drug-targetable redox-active disulphides

Protein RCC2

Intramolecular

Cysteine 395 and cysteine 437

Cysteine 280 and cysteine 305

Cysteine 209 and cysteine 261

Cysteine 261 and cysteine 337 L

Cysteine 158 and cysteine 337 L

Cysteine 158 and cysteine 261

A redox-regulated disulphide may form within Protein RCC2 between cysteines 395 and 437.

Details

Redox score ?

65

PDB code

Structure name

crystal structure of human rcc2

Structure deposition date

2016-09-12

Thiol separation (Å)

3

Half-sphere exposure sum ?

99

Minimum pK_a ?

9

% buried

100

Peptide accession

Residue number A

395

Residue number B

437

Peptide name

Protein RCC2

Ligandability

Cysteine 395 of Protein RCC2

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 437 of Protein RCC2

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 Protein RCC2 between cysteines 280 and 305. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

56

PDB code

Structure name

crystal structure of human rcc2

Structure deposition date

2016-09-12

Thiol separation (Å)

5

Half-sphere exposure sum ?

81

Minimum pK_a ?

11

% buried

56

Peptide accession

Residue number A

280

Residue number B

305

Peptide name

Protein RCC2

Ligandability

Cysteine 280 of Protein RCC2

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 Protein RCC2

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 Protein RCC2 between cysteines 209 and 261. 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

crystal structure of human rcc2

Structure deposition date

2016-09-12

Thiol separation (Å)

7

Half-sphere exposure sum ?

103

Minimum pK_a ?

13

% buried

100

Peptide accession

Residue number A

209

Residue number B

261

Peptide name

Protein RCC2

Ligandability

Cysteine 209 of Protein RCC2

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 261 of Protein RCC2

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 Protein RCC2 between cysteines 261 and 337. 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

crystal structure of human rcc2

Structure deposition date

2016-09-12

Thiol separation (Å)

7

Half-sphere exposure sum ?

102

Minimum pK_a ?

12

% buried

100

Peptide accession

Residue number A

261

Residue number B

337

Peptide name

Protein RCC2

Ligandability

Cysteine 261 of Protein RCC2

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 337 of Protein RCC2

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 Protein RCC2 between cysteines 158 and 337. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

28

PDB code

Structure name

crystal structure of human rcc2

Structure deposition date

2016-09-12

Thiol separation (Å)

9

Half-sphere exposure sum ?

94

Minimum pK_a ?

11

% buried

100

Peptide accession

Residue number A

158

Residue number B

337

Peptide name

Protein RCC2

Ligandability

Cysteine 158 of Protein RCC2

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 337 of Protein RCC2

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 Protein RCC2 between cysteines 158 and 261. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

27

PDB code

Structure name

crystal structure of human rcc2

Structure deposition date

2016-09-12

Thiol separation (Å)

9

Half-sphere exposure sum ?

92

Minimum pK_a ?

11

% buried

100

Peptide accession

Residue number A

158

Residue number B

261

Peptide name

Protein RCC2

Ligandability

Cysteine 158 of Protein RCC2

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 261 of Protein RCC2

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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