ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Desmocollin-1

Intramolecular
Cysteine 665 and cysteine 673
Cysteine 471 and cysteine 559
Cysteine 584 and cysteine 667
Cysteine 665 and cysteine 667
Cysteine 667 and cysteine 673
Cysteine 584 and cysteine 665
Cysteine 584 and cysteine 673
A redox-regulated disulphide may form within Desmocollin-1 between cysteines 665 and 673 (531 and 539 respectively in this structure).

Details

Redox score ?
88
PDB code
5iry
Structure name
crystal structure of human desmocollin-1 ectodomain
Structure deposition date
2016-03-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q08554
Residue number A
665
Residue number B
673
Peptide name
Desmocollin-1

Ligandability

Cysteine 665 of Desmocollin-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 673 of Desmocollin-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 Desmocollin-1 between cysteines 471 and 559 (337 and 425 respectively in this structure).

Details

Redox score ?
86
PDB code
5iry
Structure name
crystal structure of human desmocollin-1 ectodomain
Structure deposition date
2016-03-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q08554
Residue number A
471
Residue number B
559
Peptide name
Desmocollin-1

Ligandability

Cysteine 471 of Desmocollin-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 559 of Desmocollin-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 Desmocollin-1 between cysteines 584 and 667 (450 and 533 respectively in this structure).

Details

Redox score ?
85
PDB code
5iry
Structure name
crystal structure of human desmocollin-1 ectodomain
Structure deposition date
2016-03-15
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q08554
Residue number A
584
Residue number B
667
Peptide name
Desmocollin-1

Ligandability

Cysteine 584 of Desmocollin-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 667 of Desmocollin-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 Desmocollin-1 between cysteines 665 and 667 (531 and 533 respectively in this structure).

Details

Redox score ?
77
PDB code
5iry
Structure name
crystal structure of human desmocollin-1 ectodomain
Structure deposition date
2016-03-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q08554
Residue number A
665
Residue number B
667
Peptide name
Desmocollin-1

Ligandability

Cysteine 665 of Desmocollin-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 667 of Desmocollin-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 Desmocollin-1 between cysteines 667 and 673 (533 and 539 respectively in this structure).

Details

Redox score ?
74
PDB code
5iry
Structure name
crystal structure of human desmocollin-1 ectodomain
Structure deposition date
2016-03-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q08554
Residue number A
667
Residue number B
673
Peptide name
Desmocollin-1

Ligandability

Cysteine 667 of Desmocollin-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 673 of Desmocollin-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 Desmocollin-1 between cysteines 584 and 665 (450 and 531 respectively in this structure).

Details

Redox score ?
62
PDB code
5iry
Structure name
crystal structure of human desmocollin-1 ectodomain
Structure deposition date
2016-03-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q08554
Residue number A
584
Residue number B
665
Peptide name
Desmocollin-1

Ligandability

Cysteine 584 of Desmocollin-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 665 of Desmocollin-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 Desmocollin-1 between cysteines 584 and 673 (450 and 539 respectively in this structure).

Details

Redox score ?
61
PDB code
5iry
Structure name
crystal structure of human desmocollin-1 ectodomain
Structure deposition date
2016-03-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q08554
Residue number A
584
Residue number B
673
Peptide name
Desmocollin-1

Ligandability

Cysteine 584 of Desmocollin-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 673 of Desmocollin-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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