ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Cystic fibrosis transmembrane conductance regulator

Intramolecular
Cysteine 524 and cysteine 590
Cysteine 590 and cysteine 592
Cysteine 491 and cysteine 524
Cysteine 225 and cysteine 343
Cysteine 491 and cysteine 590
Cysteine 1400 and cysteine 1410
A redox-regulated disulphide may form within Cystic fibrosis transmembrane conductance regulator between cysteines 524 and 590.

Details

Redox score ?
70
PDB code
2bbt
Structure name
human deltaf508 nbd1 with two solublizing mutations
Structure deposition date
2005-10-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
76
Minimum pKa ?
9
% buried
100
Peptide accession
P13569
Residue number A
524
Residue number B
590
Peptide name
Cystic fibrosis transmembrane conductance regulator

Ligandability

Cysteine 524 of Cystic fibrosis transmembrane conductance regulator

Cysteine 590 of Cystic fibrosis transmembrane conductance regulator

A redox-regulated disulphide may form within Cystic fibrosis transmembrane conductance regulator between cysteines 590 and 592. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2pzf
Structure name
minimal human cftr first nucleotide binding domain as a head-to-tail dimer with delta f508
Structure deposition date
2007-05-18
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
9
% buried
70
Peptide accession
P13569
Residue number A
590
Residue number B
592
Peptide name
Cystic fibrosis transmembrane conductance regulator

Ligandability

Cysteine 590 of Cystic fibrosis transmembrane conductance regulator

Cysteine 592 of Cystic fibrosis transmembrane conductance regulator

A redox-regulated disulphide may form within Cystic fibrosis transmembrane conductance regulator between cysteines 491 and 524. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1xmi
Structure name
crystal structure of human f508a nbd1 domain with atp
Structure deposition date
2004-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
9
% buried
100
Peptide accession
P13569
Residue number A
491
Residue number B
524
Peptide name
Cystic fibrosis transmembrane conductance regulator

Ligandability

Cysteine 491 of Cystic fibrosis transmembrane conductance regulator

Cysteine 524 of Cystic fibrosis transmembrane conductance regulator

A redox-regulated disulphide may form within Cystic fibrosis transmembrane conductance regulator between cysteines 225 and 343. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
5uak
Structure name
dephosphorylated, atp-free human cystic fibrosis transmembrane conductance regulator (cftr)
Structure deposition date
2016-12-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
61
Peptide accession
P13569
Residue number A
225
Residue number B
343
Peptide name
Cystic fibrosis transmembrane conductance regulator

Ligandability

Cysteine 225 of Cystic fibrosis transmembrane conductance regulator

Cysteine 343 of Cystic fibrosis transmembrane conductance regulator

A redox-regulated disulphide may form within Cystic fibrosis transmembrane conductance regulator between cysteines 491 and 590. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
1xmi
Structure name
crystal structure of human f508a nbd1 domain with atp
Structure deposition date
2004-10-02
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
100
Peptide accession
P13569
Residue number A
491
Residue number B
590
Peptide name
Cystic fibrosis transmembrane conductance regulator

Ligandability

Cysteine 491 of Cystic fibrosis transmembrane conductance regulator

Cysteine 590 of Cystic fibrosis transmembrane conductance regulator

A redox-regulated disulphide may form within Cystic fibrosis transmembrane conductance regulator between cysteines 1400 and 1410. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
6uk1
Structure name
crystal structure of nucleotide-binding domain 2 (nbd2) of the human cystic fibrosis transmembrane conductance regulator (cftr)
Structure deposition date
2019-10-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
94
Peptide accession
P13569
Residue number A
1400
Residue number B
1410
Peptide name
Cystic fibrosis transmembrane conductance regulator

Ligandability

Cysteine 1400 of Cystic fibrosis transmembrane conductance regulator

Cysteine 1410 of Cystic fibrosis transmembrane conductance regulator

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