a tool for identifying drug-targetable redox-active disulphides

Ubiquitin-associated and SH3 domain-containing protein A

Intramolecular

Cysteine 623 and cysteine 625

Cysteine 565 and cysteine 595

Cysteine 595 and cysteine 623

Cysteine 595 and cysteine 625

A redox-regulated disulphide may form within Ubiquitin-associated and SH3 domain-containing protein A between cysteines 623 and 625.

Details

Redox score ?

68

PDB code

Structure name

structure of human sts-2 histidine phosphatase domain

Structure deposition date

2017-07-05

Thiol separation (Å)

4

Half-sphere exposure sum ?

76

Minimum pK_a ?

7

% buried

68

Peptide accession

Residue number A

623

Residue number B

625

Peptide name

Ubiquitin-associated and SH3 domain-containing protein A

Ligandability

Cysteine 623 of Ubiquitin-associated and SH3 domain-containing protein A

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 625 of Ubiquitin-associated and SH3 domain-containing protein A

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 Ubiquitin-associated and SH3 domain-containing protein A between cysteines 565 and 595.

Details

Redox score ?

64

PDB code

Structure name

structure of human sts-2 histidine phosphatase domain

Structure deposition date

2017-07-05

Thiol separation (Å)

5

Half-sphere exposure sum ?

89

Minimum pK_a ?

7

% buried

100

Peptide accession

Residue number A

565

Residue number B

595

Peptide name

Ubiquitin-associated and SH3 domain-containing protein A

Ligandability

Cysteine 565 of Ubiquitin-associated and SH3 domain-containing protein A

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 595 of Ubiquitin-associated and SH3 domain-containing protein A

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 Ubiquitin-associated and SH3 domain-containing protein A between cysteines 595 and 623. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

35

PDB code

Structure name

structure of human sts-2 histidine phosphatase domain

Structure deposition date

2017-07-05

Thiol separation (Å)

10

Half-sphere exposure sum ?

89

Minimum pK_a ?

7

% buried

86

Peptide accession

Residue number A

595

Residue number B

623

Peptide name

Ubiquitin-associated and SH3 domain-containing protein A

Ligandability

Cysteine 595 of Ubiquitin-associated and SH3 domain-containing protein A

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 623 of Ubiquitin-associated and SH3 domain-containing protein A

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 Ubiquitin-associated and SH3 domain-containing protein A between cysteines 595 and 625. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

20

PDB code

Structure name

structure of human sts-2 histidine phosphatase domain

Structure deposition date

2017-07-05

Thiol separation (Å)

10

Half-sphere exposure sum ?

82

Minimum pK_a ?

16

% buried

81

Peptide accession

Residue number A

595

Residue number B

625

Peptide name

Ubiquitin-associated and SH3 domain-containing protein A

Ligandability

Cysteine 595 of Ubiquitin-associated and SH3 domain-containing protein A

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 625 of Ubiquitin-associated and SH3 domain-containing protein A

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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