Interferon-induced protein with tetratricopeptide repeats 2
Intramolecular
Cysteine 285 and cysteine 289 L
Cysteine 54 and cysteine 73
Cysteine 289 and cysteine 290 L
Cysteine 285 and cysteine 290
Cysteine 140 and cysteine 160
4g1t A 285 A 289
A redox-regulated disulphide may form within Interferon-induced protein with tetratricopeptide repeats 2 between cysteines 285 and 289.
Details
Redox score ?
66
PDB code
4g1t
Structure name
crystal structure of interferon-stimulated gene 54
Structure deposition date
2012-07-11
Thiol separation (Å)
5
Half-sphere exposure sum ?
77
Minimum pKa ?
6
% buried
76
Peptide accession
P09913
Residue number A
285
Residue number B
289
Peptide name
Interferon-induced protein with tetratricopeptide repeats 2
Ligandability
Cysteine 285 of Interferon-induced protein with tetratricopeptide repeats 2
Cysteine 289 of Interferon-induced protein with tetratricopeptide repeats 2
4g1t A 54 A 73
A redox-regulated disulphide may form within Interferon-induced protein with tetratricopeptide repeats 2 between cysteines 54 and 73. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
55
PDB code
4g1t
Structure name
crystal structure of interferon-stimulated gene 54
Structure deposition date
2012-07-11
Thiol separation (Å)
6
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
49
Peptide accession
P09913
Residue number A
54
Residue number B
73
Peptide name
Interferon-induced protein with tetratricopeptide repeats 2
Ligandability
Cysteine 54 of Interferon-induced protein with tetratricopeptide repeats 2
Cysteine 73 of Interferon-induced protein with tetratricopeptide repeats 2
4g1t A 289 A 290
A redox-regulated disulphide may form within Interferon-induced protein with tetratricopeptide repeats 2 between cysteines 289 and 290. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
4g1t
Structure name
crystal structure of interferon-stimulated gene 54
Structure deposition date
2012-07-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
6
% buried
74
Peptide accession
P09913
Residue number A
289
Residue number B
290
Peptide name
Interferon-induced protein with tetratricopeptide repeats 2
Ligandability
Cysteine 289 of Interferon-induced protein with tetratricopeptide repeats 2
Cysteine 290 of Interferon-induced protein with tetratricopeptide repeats 2
4g1t B 285 B 290
A redox-regulated disulphide may form within Interferon-induced protein with tetratricopeptide repeats 2 between cysteines 285 and 290. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
4g1t
Structure name
crystal structure of interferon-stimulated gene 54
Structure deposition date
2012-07-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
76
Peptide accession
P09913
Residue number A
285
Residue number B
290
Peptide name
Interferon-induced protein with tetratricopeptide repeats 2
Ligandability
Cysteine 285 of Interferon-induced protein with tetratricopeptide repeats 2
Cysteine 290 of Interferon-induced protein with tetratricopeptide repeats 2
4g1t A 140 A 160
A redox-regulated disulphide may form within Interferon-induced protein with tetratricopeptide repeats 2 between cysteines 140 and 160. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
29
PDB code
4g1t
Structure name
crystal structure of interferon-stimulated gene 54
Structure deposition date
2012-07-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
75
Minimum pKa ?
14
% buried
94
Peptide accession
P09913
Residue number A
140
Residue number B
160
Peptide name
Interferon-induced protein with tetratricopeptide repeats 2
Ligandability
Cysteine 140 of Interferon-induced protein with tetratricopeptide repeats 2
Cysteine 160 of Interferon-induced protein with tetratricopeptide repeats 2
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