ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Receptor-type tyrosine-protein phosphatase C

Intermolecular
Cysteine 434 and cysteine 434
Intramolecular
Cysteine 260 and cysteine 265
Cysteine 505 and cysteine 537
Cysteine 228 and cysteine 288
Cysteine 276 and cysteine 333
Cysteine 474 and cysteine 506
Cysteine 344 and cysteine 367
Cysteine 400 and cysteine 476
Cysteine 425 and cysteine 434
Cysteine 311 and cysteine 322
A redox-regulated disulphide may form between two units of Receptor-type tyrosine-protein phosphatase C at cysteines 434 and 434 (432 and 432 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
5fmv
Structure name
crystal structure of human cd45 extracellular region, domains d1-d4
Structure deposition date
2015-11-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide A name
Receptor-type tyrosine-protein phosphatase C
Peptide B name
Receptor-type tyrosine-protein phosphatase C
Peptide A accession
P08575
Peptide B accession
P08575
Peptide A residue number
434
Peptide B residue number
434

Ligandability

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 C between cysteines 260 and 265 (258 and 263 respectively in this structure).

Details

Redox score ?
89
PDB code
5fmv
Structure name
crystal structure of human cd45 extracellular region, domains d1-d4
Structure deposition date
2015-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08575
Residue number A
260
Residue number B
265
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 260 of Receptor-type tyrosine-protein phosphatase C

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 Receptor-type tyrosine-protein phosphatase C

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 C between cysteines 505 and 537 (503 and 535 respectively in this structure).

Details

Redox score ?
88
PDB code
5fmv
Structure name
crystal structure of human cd45 extracellular region, domains d1-d4
Structure deposition date
2015-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08575
Residue number A
505
Residue number B
537
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 505 of Receptor-type tyrosine-protein phosphatase C

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 537 of Receptor-type tyrosine-protein phosphatase C

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 C between cysteines 228 and 288 (226 and 286 respectively in this structure).

Details

Redox score ?
88
PDB code
5fmv
Structure name
crystal structure of human cd45 extracellular region, domains d1-d4
Structure deposition date
2015-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08575
Residue number A
228
Residue number B
288
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 228 of Receptor-type tyrosine-protein phosphatase C

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 288 of Receptor-type tyrosine-protein phosphatase C

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 C between cysteines 276 and 333 (274 and 331 respectively in this structure).

Details

Redox score ?
87
PDB code
5fmv
Structure name
crystal structure of human cd45 extracellular region, domains d1-d4
Structure deposition date
2015-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08575
Residue number A
276
Residue number B
333
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 276 of Receptor-type tyrosine-protein phosphatase C

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 333 of Receptor-type tyrosine-protein phosphatase C

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 C between cysteines 474 and 506 (120 and 152 respectively in this structure).

Details

Redox score ?
87
PDB code
5fn8
Structure name
crystal structure of rat cd45 extracellular region, domains d3-d4
Structure deposition date
2015-11-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P04157
Residue number A
474
Residue number B
506
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 474 of Receptor-type tyrosine-protein phosphatase C

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 506 of Receptor-type tyrosine-protein phosphatase C

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 C between cysteines 344 and 367 (342 and 365 respectively in this structure).

Details

Redox score ?
86
PDB code
5fmv
Structure name
crystal structure of human cd45 extracellular region, domains d1-d4
Structure deposition date
2015-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08575
Residue number A
344
Residue number B
367
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 344 of Receptor-type tyrosine-protein phosphatase C

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 Receptor-type tyrosine-protein phosphatase C

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 C between cysteines 400 and 476 (398 and 474 respectively in this structure).

Details

Redox score ?
86
PDB code
5fmv
Structure name
crystal structure of human cd45 extracellular region, domains d1-d4
Structure deposition date
2015-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08575
Residue number A
400
Residue number B
476
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 400 of Receptor-type tyrosine-protein phosphatase C

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 476 of Receptor-type tyrosine-protein phosphatase C

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 C between cysteines 425 and 434 (423 and 432 respectively in this structure).

Details

Redox score ?
85
PDB code
5fmv
Structure name
crystal structure of human cd45 extracellular region, domains d1-d4
Structure deposition date
2015-11-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08575
Residue number A
425
Residue number B
434
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 425 of Receptor-type tyrosine-protein phosphatase C

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 434 of Receptor-type tyrosine-protein phosphatase C

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 C between cysteines 311 and 322 (94 and 105 respectively in this structure).

Details

Redox score ?
80
PDB code
5fn7
Structure name
crystal structure of human cd45 extracellular region, domains d1-d2
Structure deposition date
2015-11-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08575
Residue number A
311
Residue number B
322
Peptide name
Receptor-type tyrosine-protein phosphatase C

Ligandability

Cysteine 311 of Receptor-type tyrosine-protein phosphatase C

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 322 of Receptor-type tyrosine-protein phosphatase C

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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