ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Receptor-type tyrosine-protein phosphatase alpha

Intramolecular
Cysteine 348 and cysteine 350
Cysteine 251 and cysteine 257
Cysteine 670 and cysteine 759
Cysteine 251 and cysteine 482
Cysteine 350 and cysteine 442
Cysteine 359 and cysteine 384
Cysteine 257 and cysteine 482
Cysteine 759 and cysteine 770
A redox-regulated disulphide may form within Receptor-type tyrosine-protein phosphatase alpha between cysteines 348 and 350 (339 and 341 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
6uzt
Structure name
crystal structure of rptp alpha
Structure deposition date
2019-11-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
51
Minimum pKa ?
9
% buried
48
Peptide accession
P18433
Residue number A
348
Residue number B
350
Peptide name
Receptor-type tyrosine-protein phosphatase alpha

Ligandability

Cysteine 348 of Receptor-type tyrosine-protein phosphatase alpha

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 350 of Receptor-type tyrosine-protein phosphatase alpha

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 Receptor-type tyrosine-protein phosphatase alpha between cysteines 251 and 257 (242 and 248 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
6uzt
Structure name
crystal structure of rptp alpha
Structure deposition date
2019-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
27
Peptide accession
P18433
Residue number A
251
Residue number B
257
Peptide name
Receptor-type tyrosine-protein phosphatase alpha

Ligandability

Cysteine 251 of Receptor-type tyrosine-protein phosphatase alpha

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 257 of Receptor-type tyrosine-protein phosphatase alpha

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 Receptor-type tyrosine-protein phosphatase alpha between cysteines 670 and 759 (635 and 724 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
1p15
Structure name
crystal structure of the d2 domain of rptpa
Structure deposition date
2003-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
7
% buried
100
Peptide accession
P18052
Residue number A
670
Residue number B
759
Peptide name
Receptor-type tyrosine-protein phosphatase alpha

Ligandability

Cysteine 670 of Receptor-type tyrosine-protein phosphatase alpha

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 759 of Receptor-type tyrosine-protein phosphatase alpha

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 Receptor-type tyrosine-protein phosphatase alpha between cysteines 251 and 482 (242 and 473 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
6uzt
Structure name
crystal structure of rptp alpha
Structure deposition date
2019-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
57
Peptide accession
P18433
Residue number A
251
Residue number B
482
Peptide name
Receptor-type tyrosine-protein phosphatase alpha

Ligandability

Cysteine 251 of Receptor-type tyrosine-protein phosphatase alpha

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 482 of Receptor-type tyrosine-protein phosphatase alpha

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 Receptor-type tyrosine-protein phosphatase alpha between cysteines 350 and 442 (341 and 433 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
6uzt
Structure name
crystal structure of rptp alpha
Structure deposition date
2019-11-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
8
% buried
97
Peptide accession
P18433
Residue number A
350
Residue number B
442
Peptide name
Receptor-type tyrosine-protein phosphatase alpha

Ligandability

Cysteine 350 of Receptor-type tyrosine-protein phosphatase alpha

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 442 of Receptor-type tyrosine-protein phosphatase alpha

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 Receptor-type tyrosine-protein phosphatase alpha between cysteines 359 and 384 (350 and 375 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6uzt
Structure name
crystal structure of rptp alpha
Structure deposition date
2019-11-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
9
% buried
9
Peptide accession
P18433
Residue number A
359
Residue number B
384
Peptide name
Receptor-type tyrosine-protein phosphatase alpha

Ligandability

Cysteine 359 of Receptor-type tyrosine-protein phosphatase alpha

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 384 of Receptor-type tyrosine-protein phosphatase alpha

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 Receptor-type tyrosine-protein phosphatase alpha between cysteines 257 and 482 (248 and 473 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6uzt
Structure name
crystal structure of rptp alpha
Structure deposition date
2019-11-15
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
77
Peptide accession
P18433
Residue number A
257
Residue number B
482
Peptide name
Receptor-type tyrosine-protein phosphatase alpha

Ligandability

Cysteine 257 of Receptor-type tyrosine-protein phosphatase alpha

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 482 of Receptor-type tyrosine-protein phosphatase alpha

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 Receptor-type tyrosine-protein phosphatase alpha between cysteines 759 and 770 (724 and 735 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
1p15
Structure name
crystal structure of the d2 domain of rptpa
Structure deposition date
2003-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
93
Minimum pKa ?
7
% buried
100
Peptide accession
P18052
Residue number A
759
Residue number B
770
Peptide name
Receptor-type tyrosine-protein phosphatase alpha

Ligandability

Cysteine 759 of Receptor-type tyrosine-protein phosphatase alpha

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 770 of Receptor-type tyrosine-protein phosphatase alpha

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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