ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Claudin-4

Intramolecular
Cysteine 54 and cysteine 64
Cysteine 182 and cysteine 183
Cysteine 183 and cysteine 185
Cysteine 104 and cysteine 107
Cysteine 24 and cysteine 25
A redox-regulated disulphide may form within Claudin-4 between cysteines 54 and 64.

Details

Redox score ?
81
PDB code
7kp4
Structure name
crystal structure of human claudin-4 in complex with clostridium perfringens enterotoxin c-terminal domain
Structure deposition date
2020-11-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
O14493
Residue number A
54
Residue number B
64
Peptide name
Claudin-4

Ligandability

Cysteine 54 of Claudin-4

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 64 of Claudin-4

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 Claudin-4 between cysteines 182 and 183 (1345 and 1346 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
5b2g
Structure name
crystal structure of human claudin-4 in complex with c-terminal fragment of clostridium perfringens enterotoxin
Structure deposition date
2016-01-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
47
Minimum pKa ?
9
% buried
11
Peptide accession
O14493
Residue number A
182
Residue number B
183
Peptide name
Claudin-4

Ligandability

Cysteine 182 of Claudin-4

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 183 of Claudin-4

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 Claudin-4 between cysteines 183 and 185. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
7kp4
Structure name
crystal structure of human claudin-4 in complex with clostridium perfringens enterotoxin c-terminal domain
Structure deposition date
2020-11-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
0
Peptide accession
O14493
Residue number A
183
Residue number B
185
Peptide name
Claudin-4

Ligandability

Cysteine 183 of Claudin-4

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 185 of Claudin-4

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 Claudin-4 between cysteines 104 and 107. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5b2g
Structure name
crystal structure of human claudin-4 in complex with c-terminal fragment of clostridium perfringens enterotoxin
Structure deposition date
2016-01-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
10
% buried
44
Peptide accession
O14493
Residue number A
104
Residue number B
107
Peptide name
Claudin-4

Ligandability

Cysteine 104 of Claudin-4

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 107 of Claudin-4

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 Claudin-4 between cysteines 24 and 25 (1187 and 1188 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
5b2g
Structure name
crystal structure of human claudin-4 in complex with c-terminal fragment of clostridium perfringens enterotoxin
Structure deposition date
2016-01-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
98
Peptide accession
O14493
Residue number A
24
Residue number B
25
Peptide name
Claudin-4

Ligandability

Cysteine 24 of Claudin-4

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 25 of Claudin-4

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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