ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Tight junction protein ZO-1

Intramolecular
Cysteine 1718 and cysteine 1740
Cysteine 1676 and cysteine 1718
A redox-regulated disulphide may form within Tight junction protein ZO-1 between cysteines 1718 and 1740 (88 and 110 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
2kxr
Structure name
zo1 zu5 domain mc/aa mutation
Structure deposition date
2010-05-12
Thiol separation (Å)
8
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
8
Peptide accession
Q07157
Residue number A
1718
Residue number B
1740
Peptide name
Tight junction protein ZO-1

Ligandability

Cysteine 1718 of Tight junction protein ZO-1

Cysteine 1740 of Tight junction protein ZO-1

A redox-regulated disulphide may form within Tight junction protein ZO-1 between cysteines 1676 and 1718 (46 and 88 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
2kxr
Structure name
zo1 zu5 domain mc/aa mutation
Structure deposition date
2010-05-12
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
9
% buried
4
Peptide accession
Q07157
Residue number A
1676
Residue number B
1718
Peptide name
Tight junction protein ZO-1

Ligandability

Cysteine 1676 of Tight junction protein ZO-1

Cysteine 1718 of Tight junction protein ZO-1

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