Insulin-like growth factor-binding protein 2
Intramolecular
Cysteine 227 and cysteine 261
Cysteine 285 and cysteine 306 L
Cysteine 272 and cysteine 283 L
Cysteine 283 and cysteine 306 L
Cysteine 272 and cysteine 306
Cysteine 272 and cysteine 285 L
Cysteine 283 and cysteine 285 L
2h7t A 191 A 225
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 2 between cysteines 227 and 261 (191 and 225 respectively in this structure).
Details
Redox score ?
87
PDB code
2h7t
Structure name
solution structure of the c-terminal domain of insulin-like growth factor binding protein 2 (igfbp-2)
Structure deposition date
2006-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18065
Residue number A
227
Residue number B
261
Peptide name
Insulin-like growth factor-binding protein 2
Ligandability
Cysteine 227 of Insulin-like growth factor-binding protein 2
Cysteine 261 of Insulin-like growth factor-binding protein 2
2h7t A 249 A 270
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 2 between cysteines 285 and 306 (249 and 270 respectively in this structure).
Details
Redox score ?
84
PDB code
2h7t
Structure name
solution structure of the c-terminal domain of insulin-like growth factor binding protein 2 (igfbp-2)
Structure deposition date
2006-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18065
Residue number A
285
Residue number B
306
Peptide name
Insulin-like growth factor-binding protein 2
Ligandability
Cysteine 285 of Insulin-like growth factor-binding protein 2
Cysteine 306 of Insulin-like growth factor-binding protein 2
2h7t A 236 A 247
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 2 between cysteines 272 and 283 (236 and 247 respectively in this structure).
Details
Redox score ?
81
PDB code
2h7t
Structure name
solution structure of the c-terminal domain of insulin-like growth factor binding protein 2 (igfbp-2)
Structure deposition date
2006-06-03
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18065
Residue number A
272
Residue number B
283
Peptide name
Insulin-like growth factor-binding protein 2
Ligandability
Cysteine 272 of Insulin-like growth factor-binding protein 2
Cysteine 283 of Insulin-like growth factor-binding protein 2
2h7t A 247 A 270
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 2 between cysteines 283 and 306 (247 and 270 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
2h7t
Structure name
solution structure of the c-terminal domain of insulin-like growth factor binding protein 2 (igfbp-2)
Structure deposition date
2006-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18065
Residue number A
283
Residue number B
306
Peptide name
Insulin-like growth factor-binding protein 2
Ligandability
Cysteine 283 of Insulin-like growth factor-binding protein 2
Cysteine 306 of Insulin-like growth factor-binding protein 2
2h7t A 236 A 270
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 2 between cysteines 272 and 306 (236 and 270 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2h7t
Structure name
solution structure of the c-terminal domain of insulin-like growth factor binding protein 2 (igfbp-2)
Structure deposition date
2006-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18065
Residue number A
272
Residue number B
306
Peptide name
Insulin-like growth factor-binding protein 2
Ligandability
Cysteine 272 of Insulin-like growth factor-binding protein 2
Cysteine 306 of Insulin-like growth factor-binding protein 2
2h7t A 236 A 249
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 2 between cysteines 272 and 285 (236 and 249 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
37
PDB code
2h7t
Structure name
solution structure of the c-terminal domain of insulin-like growth factor binding protein 2 (igfbp-2)
Structure deposition date
2006-06-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18065
Residue number A
272
Residue number B
285
Peptide name
Insulin-like growth factor-binding protein 2
Ligandability
Cysteine 272 of Insulin-like growth factor-binding protein 2
Cysteine 285 of Insulin-like growth factor-binding protein 2
2h7t A 247 A 249
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 2 between cysteines 283 and 285 (247 and 249 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2h7t
Structure name
solution structure of the c-terminal domain of insulin-like growth factor binding protein 2 (igfbp-2)
Structure deposition date
2006-06-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P18065
Residue number A
283
Residue number B
285
Peptide name
Insulin-like growth factor-binding protein 2
Ligandability
Cysteine 283 of Insulin-like growth factor-binding protein 2
Cysteine 285 of Insulin-like growth factor-binding protein 2
If this tool was useful for finding a disulphide, please cite: