Glutaredoxin-1
Intramolecular
Cysteine 23 and cysteine 26 L
Cysteine 23 and cysteine 83 L
Cysteine 26 and cysteine 83 L
1jhb A 23 A 26
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
4rqr A 22 A 82
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
4rqr A 25 A 82
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
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