ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Desmoglein-2

Intramolecular
Cysteine 507 and cysteine 593
Cysteine 591 and cysteine 599
Cysteine 496 and cysteine 580
Cysteine 591 and cysteine 593
Cysteine 593 and cysteine 599
Cysteine 507 and cysteine 591
Cysteine 507 and cysteine 599
A redox-regulated disulphide may form within Desmoglein-2 between cysteines 507 and 593 (458 and 544 respectively in this structure).

Details

Redox score ?
86
PDB code
5erd
Structure name
crystal structure of human desmoglein-2 ectodomain
Structure deposition date
2015-11-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14126
Residue number A
507
Residue number B
593
Peptide name
Desmoglein-2

Ligandability

Cysteine 507 of Desmoglein-2

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 593 of Desmoglein-2

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 Desmoglein-2 between cysteines 591 and 599 (540 and 548 respectively in this structure).

Details

Redox score ?
85
PDB code
5j5j
Structure name
crystal structure of a chimera of human desmocollin-2 ec1 and human desmoglein-2 ec2-ec5
Structure deposition date
2016-04-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14126
Residue number A
591
Residue number B
599
Peptide name
Desmoglein-2

Ligandability

Cysteine 591 of Desmoglein-2

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 599 of Desmoglein-2

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 Desmoglein-2 between cysteines 496 and 580 (445 and 529 respectively in this structure).

Details

Redox score ?
85
PDB code
5j5j
Structure name
crystal structure of a chimera of human desmocollin-2 ec1 and human desmoglein-2 ec2-ec5
Structure deposition date
2016-04-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14126
Residue number A
496
Residue number B
580
Peptide name
Desmoglein-2

Ligandability

Cysteine 496 of Desmoglein-2

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 580 of Desmoglein-2

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 Desmoglein-2 between cysteines 591 and 593 (542 and 544 respectively in this structure).

Details

Redox score ?
79
PDB code
5erd
Structure name
crystal structure of human desmoglein-2 ectodomain
Structure deposition date
2015-11-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14126
Residue number A
591
Residue number B
593
Peptide name
Desmoglein-2

Ligandability

Cysteine 591 of Desmoglein-2

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 593 of Desmoglein-2

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 Desmoglein-2 between cysteines 593 and 599 (542 and 548 respectively in this structure).

Details

Redox score ?
72
PDB code
5j5j
Structure name
crystal structure of a chimera of human desmocollin-2 ec1 and human desmoglein-2 ec2-ec5
Structure deposition date
2016-04-02
Thiol separation (Å)
5
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14126
Residue number A
593
Residue number B
599
Peptide name
Desmoglein-2

Ligandability

Cysteine 593 of Desmoglein-2

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 599 of Desmoglein-2

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 Desmoglein-2 between cysteines 507 and 591 (458 and 542 respectively in this structure).

Details

Redox score ?
68
PDB code
5erd
Structure name
crystal structure of human desmoglein-2 ectodomain
Structure deposition date
2015-11-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14126
Residue number A
507
Residue number B
591
Peptide name
Desmoglein-2

Ligandability

Cysteine 507 of Desmoglein-2

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 591 of Desmoglein-2

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 Desmoglein-2 between cysteines 507 and 599 (458 and 550 respectively in this structure).

Details

Redox score ?
62
PDB code
5erd
Structure name
crystal structure of human desmoglein-2 ectodomain
Structure deposition date
2015-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q14126
Residue number A
507
Residue number B
599
Peptide name
Desmoglein-2

Ligandability

Cysteine 507 of Desmoglein-2

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 599 of Desmoglein-2

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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