ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Plakophilin-1

Intramolecular
Cysteine 461 and cysteine 467
Cysteine 662 and cysteine 692
Cysteine 461 and cysteine 475
Cysteine 467 and cysteine 568
Cysteine 477 and cysteine 568
Cysteine 475 and cysteine 477
A redox-regulated disulphide may form within Plakophilin-1 between cysteines 461 and 467 (440 and 446 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1xm9
Structure name
structure of the armadillo repeat domain of plakophilin 1
Structure deposition date
2004-10-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
37
Peptide accession
Q13835
Residue number A
461
Residue number B
467
Peptide name
Plakophilin-1

Ligandability

Cysteine 461 of Plakophilin-1

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 467 of Plakophilin-1

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 Plakophilin-1 between cysteines 662 and 692 (641 and 671 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
1xm9
Structure name
structure of the armadillo repeat domain of plakophilin 1
Structure deposition date
2004-10-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
10
% buried
61
Peptide accession
Q13835
Residue number A
662
Residue number B
692
Peptide name
Plakophilin-1

Ligandability

Cysteine 662 of Plakophilin-1

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 692 of Plakophilin-1

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 Plakophilin-1 between cysteines 461 and 475 (440 and 454 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
1xm9
Structure name
structure of the armadillo repeat domain of plakophilin 1
Structure deposition date
2004-10-01
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
75
Peptide accession
Q13835
Residue number A
461
Residue number B
475
Peptide name
Plakophilin-1

Ligandability

Cysteine 461 of Plakophilin-1

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 475 of Plakophilin-1

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 Plakophilin-1 between cysteines 467 and 568 (446 and 547 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
1xm9
Structure name
structure of the armadillo repeat domain of plakophilin 1
Structure deposition date
2004-10-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
10
% buried
62
Peptide accession
Q13835
Residue number A
467
Residue number B
568
Peptide name
Plakophilin-1

Ligandability

Cysteine 467 of Plakophilin-1

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 568 of Plakophilin-1

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 Plakophilin-1 between cysteines 477 and 568 (456 and 547 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
1xm9
Structure name
structure of the armadillo repeat domain of plakophilin 1
Structure deposition date
2004-10-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
90
Peptide accession
Q13835
Residue number A
477
Residue number B
568
Peptide name
Plakophilin-1

Ligandability

Cysteine 477 of Plakophilin-1

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 568 of Plakophilin-1

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 Plakophilin-1 between cysteines 475 and 477 (454 and 456 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
1xm9
Structure name
structure of the armadillo repeat domain of plakophilin 1
Structure deposition date
2004-10-01
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
90
Peptide accession
Q13835
Residue number A
475
Residue number B
477
Peptide name
Plakophilin-1

Ligandability

Cysteine 475 of Plakophilin-1

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 477 of Plakophilin-1

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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