Insulin-like growth factor-binding protein 1
Intermolecular
Cysteine 96 of Insulin-like growth factor I and cysteine 206
Cysteine 54 of Insulin-like growth factor I and cysteine 206
Cysteine 54 of Insulin-like growth factor I and cysteine 176
Cysteine 96 of Insulin-like growth factor I and cysteine 176
Intramolecular
Cysteine 230 and cysteine 251
Cysteine 217 and cysteine 228
Cysteine 176 and cysteine 206
Cysteine 217 and cysteine 251
Cysteine 228 and cysteine 251
Cysteine 228 and cysteine 230
Cysteine 217 and cysteine 230
2dsq I 48 G 181
A redox-regulated disulphide may form between cysteine 96 of Insulin-like growth factor I and cysteine 206 of Insulin-like growth factor-binding protein 1 (48 and 181 respectively in this structure).
Details
Redox score ?
61
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor I
Peptide B name
Insulin-like growth factor-binding protein 1
Peptide A accession
P05019
Peptide B accession
P08833
Peptide A residue number
96
Peptide B residue number
206
Ligandability
Cysteine 96 of Insulin-like growth factor I
Cysteine 206 of Insulin-like growth factor-binding protein 1
2dsq I 6 G 181
A redox-regulated disulphide may form between cysteine 54 of Insulin-like growth factor I and cysteine 206 of Insulin-like growth factor-binding protein 1 (6 and 181 respectively in this structure).
Details
Redox score ?
61
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor I
Peptide B name
Insulin-like growth factor-binding protein 1
Peptide A accession
P05019
Peptide B accession
P08833
Peptide A residue number
54
Peptide B residue number
206
Ligandability
Cysteine 54 of Insulin-like growth factor I
Cysteine 206 of Insulin-like growth factor-binding protein 1
2dsq C 6 H 151
A redox-regulated disulphide may form between cysteine 54 of Insulin-like growth factor I and cysteine 176 of Insulin-like growth factor-binding protein 1 (6 and 151 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor I
Peptide B name
Insulin-like growth factor-binding protein 1
Peptide A accession
P05019
Peptide B accession
P08833
Peptide A residue number
54
Peptide B residue number
176
Ligandability
Cysteine 54 of Insulin-like growth factor I
Cysteine 176 of Insulin-like growth factor-binding protein 1
2dsq I 48 G 151
A redox-regulated disulphide may form between cysteine 96 of Insulin-like growth factor I and cysteine 176 of Insulin-like growth factor-binding protein 1 (48 and 151 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
53
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor I
Peptide B name
Insulin-like growth factor-binding protein 1
Peptide A accession
P05019
Peptide B accession
P08833
Peptide A residue number
96
Peptide B residue number
176
Ligandability
Cysteine 96 of Insulin-like growth factor I
Cysteine 176 of Insulin-like growth factor-binding protein 1
2dsq H 205 H 226
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 1 between cysteines 230 and 251 (205 and 226 respectively in this structure).
Details
Redox score ?
87
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08833
Residue number A
230
Residue number B
251
Peptide name
Insulin-like growth factor-binding protein 1
Ligandability
Cysteine 230 of Insulin-like growth factor-binding protein 1
Cysteine 251 of Insulin-like growth factor-binding protein 1
2dsq H 192 H 203
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 1 between cysteines 217 and 228 (192 and 203 respectively in this structure).
Details
Redox score ?
85
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
3
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
30
Peptide accession
P08833
Residue number A
217
Residue number B
228
Peptide name
Insulin-like growth factor-binding protein 1
Ligandability
Cysteine 217 of Insulin-like growth factor-binding protein 1
Cysteine 228 of Insulin-like growth factor-binding protein 1
2dsq G 151 G 181
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 1 between cysteines 176 and 206 (151 and 181 respectively in this structure).
Details
Redox score ?
83
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08833
Residue number A
176
Residue number B
206
Peptide name
Insulin-like growth factor-binding protein 1
Ligandability
Cysteine 176 of Insulin-like growth factor-binding protein 1
Cysteine 206 of Insulin-like growth factor-binding protein 1
2dsq H 192 H 226
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 1 between cysteines 217 and 251 (192 and 226 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
nan
Peptide accession
P08833
Residue number A
217
Residue number B
251
Peptide name
Insulin-like growth factor-binding protein 1
Ligandability
Cysteine 217 of Insulin-like growth factor-binding protein 1
Cysteine 251 of Insulin-like growth factor-binding protein 1
2dsq G 203 G 226
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 1 between cysteines 228 and 251 (203 and 226 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08833
Residue number A
228
Residue number B
251
Peptide name
Insulin-like growth factor-binding protein 1
Ligandability
Cysteine 228 of Insulin-like growth factor-binding protein 1
Cysteine 251 of Insulin-like growth factor-binding protein 1
2dsq G 203 G 205
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 1 between cysteines 228 and 230 (203 and 205 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
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P08833
Residue number A
228
Residue number B
230
Peptide name
Insulin-like growth factor-binding protein 1
Ligandability
Cysteine 228 of Insulin-like growth factor-binding protein 1
Cysteine 230 of Insulin-like growth factor-binding protein 1
2dsq H 192 H 205
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 1 between cysteines 217 and 230 (192 and 205 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2dsq
Structure name
structural basis for the inhibition of insulin-like growth factors by igf binding proteins
Structure deposition date
2006-07-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
12
% buried
nan
Peptide accession
P08833
Residue number A
217
Residue number B
230
Peptide name
Insulin-like growth factor-binding protein 1
Ligandability
Cysteine 217 of Insulin-like growth factor-binding protein 1
Cysteine 230 of Insulin-like growth factor-binding protein 1
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