ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cadherin-6

Intramolecular
Cysteine 497 and cysteine 591
Cysteine 589 and cysteine 591
Cysteine 497 and cysteine 589
A redox-regulated disulphide may form within Cadherin-6 between cysteines 497 and 591.

Details

Redox score ?
86
PDB code
5veb
Structure name
crystal structure of a fab binding to extracellular domain 5 of cadherin-6
Structure deposition date
2017-04-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P55285
Residue number A
497
Residue number B
591
Peptide name
Cadherin-6

Ligandability

Cysteine 497 of Cadherin-6

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 Cadherin-6

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 Cadherin-6 between cysteines 589 and 591.

Details

Redox score ?
66
PDB code
5veb
Structure name
crystal structure of a fab binding to extracellular domain 5 of cadherin-6
Structure deposition date
2017-04-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
P55285
Residue number A
589
Residue number B
591
Peptide name
Cadherin-6

Ligandability

Cysteine 589 of Cadherin-6

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 Cadherin-6

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 Cadherin-6 between cysteines 497 and 589. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
52
PDB code
5veb
Structure name
crystal structure of a fab binding to extracellular domain 5 of cadherin-6
Structure deposition date
2017-04-04
Thiol separation (Å)
7
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
nan
Peptide accession
P55285
Residue number A
497
Residue number B
589
Peptide name
Cadherin-6

Ligandability

Cysteine 497 of Cadherin-6

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 589 of Cadherin-6

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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