a tool for identifying drug-targetable redox-active disulphides

Tyrosine-protein phosphatase non-receptor type 11

Intramolecular

Cysteine 367 and cysteine 459

Cysteine 333 and cysteine 367

Cysteine 104 and cysteine 174

Cysteine 333 and cysteine 459

A redox-regulated disulphide may form within Tyrosine-protein phosphatase non-receptor type 11 between cysteines 367 and 459.

Details

Redox score ?

78

PDB code

Structure name

small-molecule allosteric regulation mechanism of shp2

Structure deposition date

2022-04-09

Thiol separation (Å)

3

Half-sphere exposure sum ?

77

Minimum pK_a ?

7

% buried

100

Peptide accession

Residue number A

367

Residue number B

459

Peptide name

Tyrosine-protein phosphatase non-receptor type 11

Ligandability

Cysteine 367 of Tyrosine-protein phosphatase non-receptor type 11

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 459 of Tyrosine-protein phosphatase non-receptor type 11

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 Tyrosine-protein phosphatase non-receptor type 11 between cysteines 333 and 367.

Details

Redox score ?

75

PDB code

Structure name

structure of human shp2 in complex with compound 27

Structure deposition date

2021-06-24

Thiol separation (Å)

4

Half-sphere exposure sum ?

72

Minimum pK_a ?

5

% buried

100

Peptide accession

Residue number A

333

Residue number B

367

Peptide name

Tyrosine-protein phosphatase non-receptor type 11

Ligandability

Cysteine 333 of Tyrosine-protein phosphatase non-receptor type 11

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 367 of Tyrosine-protein phosphatase non-receptor type 11

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 Tyrosine-protein phosphatase non-receptor type 11 between cysteines 104 and 174. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

44

PDB code

Structure name

crystal structure of shp2_sh2-caga epiya_c peptide complex

Structure deposition date

2017-02-24

Thiol separation (Å)

9

Half-sphere exposure sum ?

60

Minimum pK_a ?

11

% buried

54

Peptide accession

Residue number A

104

Residue number B

174

Peptide name

Tyrosine-protein phosphatase non-receptor type 11

Ligandability

Cysteine 104 of Tyrosine-protein phosphatase non-receptor type 11

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 174 of Tyrosine-protein phosphatase non-receptor type 11

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 Tyrosine-protein phosphatase non-receptor type 11 between cysteines 333 and 459. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

44

PDB code

Structure name

small-molecule allosteric regulation mechanism of shp2

Structure deposition date

2022-04-09

Thiol separation (Å)

8

Half-sphere exposure sum ?

78

Minimum pK_a ?

8

% buried

100

Peptide accession

Residue number A

333

Residue number B

459

Peptide name

Tyrosine-protein phosphatase non-receptor type 11

Ligandability

Cysteine 333 of Tyrosine-protein phosphatase non-receptor type 11

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 459 of Tyrosine-protein phosphatase non-receptor type 11

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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