Glutaredoxin-2, mitochondrial
Intermolecular
Cysteine 77 and cysteine 77
Intramolecular
Cysteine 68 and cysteine 153
Cysteine 77 and cysteine 80
2ht9 A 37 B 37
A redox-regulated disulphide may form between two units of Glutaredoxin-2, mitochondrial at cysteines 77 and 77 (37 and 37 respectively in this structure).
Details
Redox score ?
64
PDB code
2ht9
Structure name
the structure of dimeric human glutaredoxin 2
Structure deposition date
2006-07-25
Thiol separation (Å)
7
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
72
Peptide A name
Glutaredoxin-2, mitochondrial
Peptide B name
Glutaredoxin-2, mitochondrial
Peptide A accession
Q9NS18
Peptide B accession
Q9NS18
Peptide A residue number
77
Peptide B residue number
77
Ligandability
2ht9 A 28 A 113
A redox-regulated disulphide may form within Glutaredoxin-2, mitochondrial between cysteines 68 and 153 (28 and 113 respectively in this structure).
Details
Redox score ?
85
PDB code
2ht9
Structure name
the structure of dimeric human glutaredoxin 2
Structure deposition date
2006-07-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9NS18
Residue number A
68
Residue number B
153
Peptide name
Glutaredoxin-2, mitochondrial
Ligandability
Cysteine 68 of Glutaredoxin-2, mitochondrial
Cysteine 153 of Glutaredoxin-2, mitochondrial
2ht9 A 37 A 40
A redox-regulated disulphide may form within Glutaredoxin-2, mitochondrial between cysteines 77 and 80 (37 and 40 respectively in this structure).
Details
Redox score ?
79
PDB code
2ht9
Structure name
the structure of dimeric human glutaredoxin 2
Structure deposition date
2006-07-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
84
Peptide accession
Q9NS18
Residue number A
77
Residue number B
80
Peptide name
Glutaredoxin-2, mitochondrial
Ligandability
Cysteine 77 of Glutaredoxin-2, mitochondrial
Cysteine 80 of Glutaredoxin-2, mitochondrial
If this tool was useful for finding a disulphide, please cite: