ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Glutaredoxin-1

Intramolecular
Cysteine 23 and cysteine 26 L
Cysteine 23 and cysteine 83 L
Cysteine 26 and cysteine 83 L
A redox-regulated disulphide may form within Glutaredoxin-1 between cysteines 23 and 26.

Details

Redox score ?
81
PDB code
1jhb
Structure name
human glutaredoxin in fully reduced form, nmr, 20 structures
Structure deposition date
1998-02-17
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
8
% buried
28
Peptide accession
P35754
Residue number A
23
Residue number B
26
Peptide name
Glutaredoxin-1

Ligandability

Cysteine 23 of Glutaredoxin-1

Cysteine 26 of Glutaredoxin-1

A redox-regulated disulphide may form within Glutaredoxin-1 between cysteines 23 and 83 (22 and 82 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
4rqr
Structure name
crystal structure of human glutaredoxin with mesna
Structure deposition date
2014-11-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35754
Residue number A
23
Residue number B
83
Peptide name
Glutaredoxin-1

Ligandability

Cysteine 23 of Glutaredoxin-1

Cysteine 83 of Glutaredoxin-1

A redox-regulated disulphide may form within Glutaredoxin-1 between cysteines 26 and 83 (25 and 82 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4rqr
Structure name
crystal structure of human glutaredoxin with mesna
Structure deposition date
2014-11-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35754
Residue number A
26
Residue number B
83
Peptide name
Glutaredoxin-1

Ligandability

Cysteine 26 of Glutaredoxin-1

Cysteine 83 of Glutaredoxin-1

If this tool was useful for finding a disulphide, please cite: