Insulin-like growth factor-binding protein 4
Intermolecular
Cysteine 204 and cysteine 54 of Insulin-like growth factor I
Cysteine 174 and cysteine 54 of Insulin-like growth factor I
Cysteine 204 and cysteine 96 of Insulin-like growth factor I
Cysteine 174 and cysteine 96 of Insulin-like growth factor I
Intramolecular
Cysteine 38 and cysteine 56
Cysteine 44 and cysteine 59
Cysteine 30 and cysteine 55
Cysteine 27 and cysteine 53
Cysteine 228 and cysteine 249
Cysteine 74 and cysteine 100
More...Cysteine 215 and cysteine 226
Cysteine 174 and cysteine 204
Cysteine 67 and cysteine 80
Cysteine 67 and cysteine 100
Cysteine 67 and cysteine 74
Cysteine 74 and cysteine 80
Cysteine 80 and cysteine 100
Cysteine 55 and cysteine 56
Cysteine 38 and cysteine 55
Cysteine 30 and cysteine 38
Cysteine 27 and cysteine 30
Cysteine 226 and cysteine 249
Cysteine 27 and cysteine 55
Cysteine 30 and cysteine 56
Cysteine 30 and cysteine 53
Cysteine 215 and cysteine 249
Cysteine 53 and cysteine 55
Cysteine 226 and cysteine 228
Cysteine 215 and cysteine 228
2dsr G 183 I 6
A redox-regulated disulphide may form between cysteine 204 of Insulin-like growth factor-binding protein 4 and cysteine 54 of Insulin-like growth factor I (183 and 6 respectively in this structure).
Details
Redox score ?
66
PDB code
2dsr
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 ?
87
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor-binding protein 4
Peptide B name
Insulin-like growth factor I
Peptide A accession
P22692
Peptide B accession
P05019
Peptide A residue number
204
Peptide B residue number
54
Ligandability
Cysteine 204 of Insulin-like growth factor-binding protein 4
Cysteine 54 of Insulin-like growth factor I
2dsr G 153 I 6
A redox-regulated disulphide may form between cysteine 174 of Insulin-like growth factor-binding protein 4 and cysteine 54 of Insulin-like growth factor I (153 and 6 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2dsr
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-binding protein 4
Peptide B name
Insulin-like growth factor I
Peptide A accession
P22692
Peptide B accession
P05019
Peptide A residue number
174
Peptide B residue number
54
Ligandability
Cysteine 174 of Insulin-like growth factor-binding protein 4
Cysteine 54 of Insulin-like growth factor I
2dsr G 183 I 48
A redox-regulated disulphide may form between cysteine 204 of Insulin-like growth factor-binding protein 4 and cysteine 96 of Insulin-like growth factor I (183 and 48 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
2dsr
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 ?
79
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor-binding protein 4
Peptide B name
Insulin-like growth factor I
Peptide A accession
P22692
Peptide B accession
P05019
Peptide A residue number
204
Peptide B residue number
96
Ligandability
Cysteine 204 of Insulin-like growth factor-binding protein 4
Cysteine 96 of Insulin-like growth factor I
2dsr G 153 I 48
A redox-regulated disulphide may form between cysteine 174 of Insulin-like growth factor-binding protein 4 and cysteine 96 of Insulin-like growth factor I (153 and 48 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
2dsr
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-binding protein 4
Peptide B name
Insulin-like growth factor I
Peptide A accession
P22692
Peptide B accession
P05019
Peptide A residue number
174
Peptide B residue number
96
Ligandability
Cysteine 174 of Insulin-like growth factor-binding protein 4
Cysteine 96 of Insulin-like growth factor I
2dsq B 17 B 35
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 38 and 56 (17 and 35 respectively in this structure).
Details
Redox score ?
88
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 ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
38
Residue number B
56
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 38 of Insulin-like growth factor-binding protein 4
Cysteine 56 of Insulin-like growth factor-binding protein 4
2dsp B 23 B 38
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 44 and 59 (23 and 38 respectively in this structure).
Details
Redox score ?
87
PDB code
2dsp
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 ?
40
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
44
Residue number B
59
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 44 of Insulin-like growth factor-binding protein 4
Cysteine 59 of Insulin-like growth factor-binding protein 4
2dsq B 9 B 34
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 30 and 55 (9 and 34 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 ?
43
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
30
Residue number B
55
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 30 of Insulin-like growth factor-binding protein 4
Cysteine 55 of Insulin-like growth factor-binding protein 4
2dsq A 6 A 32
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 27 and 53 (6 and 32 respectively in this structure).
Details
Redox score ?
86
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 ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
27
Residue number B
53
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 27 of Insulin-like growth factor-binding protein 4
Cysteine 53 of Insulin-like growth factor-binding protein 4
2dsr G 207 G 228
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 228 and 249 (207 and 228 respectively in this structure).
Details
Redox score ?
86
PDB code
2dsr
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 ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
228
Residue number B
249
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 228 of Insulin-like growth factor-binding protein 4
Cysteine 249 of Insulin-like growth factor-binding protein 4
2dsr B 53 B 79
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 74 and 100 (53 and 79 respectively in this structure).
Details
Redox score ?
85
PDB code
2dsr
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 ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
74
Residue number B
100
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 74 of Insulin-like growth factor-binding protein 4
Cysteine 100 of Insulin-like growth factor-binding protein 4
2dsr G 194 G 205
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 215 and 226 (194 and 205 respectively in this structure).
Details
Redox score ?
84
PDB code
2dsr
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 ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
215
Residue number B
226
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 215 of Insulin-like growth factor-binding protein 4
Cysteine 226 of Insulin-like growth factor-binding protein 4
2dsr G 153 G 183
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 174 and 204 (153 and 183 respectively in this structure).
Details
Redox score ?
83
PDB code
2dsr
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 ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
174
Residue number B
204
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 174 of Insulin-like growth factor-binding protein 4
Cysteine 204 of Insulin-like growth factor-binding protein 4
2dsp B 46 B 59
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 67 and 80 (46 and 59 respectively in this structure).
Details
Redox score ?
83
PDB code
2dsp
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 ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
67
Residue number B
80
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 67 of Insulin-like growth factor-binding protein 4
Cysteine 80 of Insulin-like growth factor-binding protein 4
2dsq B 46 B 79
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 67 and 100 (46 and 79 respectively in this structure).
Details
Redox score ?
74
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)
4
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
67
Residue number B
100
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 67 of Insulin-like growth factor-binding protein 4
Cysteine 100 of Insulin-like growth factor-binding protein 4
2dsp B 46 B 53
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 67 and 74 (46 and 53 respectively in this structure).
Details
Redox score ?
72
PDB code
2dsp
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)
4
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
67
Residue number B
74
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 67 of Insulin-like growth factor-binding protein 4
Cysteine 74 of Insulin-like growth factor-binding protein 4
2dsp B 53 B 59
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 74 and 80 (53 and 59 respectively in this structure).
Details
Redox score ?
67
PDB code
2dsp
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 ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
74
Residue number B
80
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 74 of Insulin-like growth factor-binding protein 4
Cysteine 80 of Insulin-like growth factor-binding protein 4
2dsp B 59 B 79
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 80 and 100 (59 and 79 respectively in this structure).
Details
Redox score ?
64
PDB code
2dsp
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 ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
80
Residue number B
100
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 80 of Insulin-like growth factor-binding protein 4
Cysteine 100 of Insulin-like growth factor-binding protein 4
1wqj B 34 B 35
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 55 and 56 (34 and 35 respectively in this structure).
Details
Redox score ?
61
PDB code
1wqj
Structure name
structural basis for the regulation of insulin-like growth factors (igfs) by igf binding proteins (igfbps)
Structure deposition date
2004-09-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
55
Residue number B
56
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 55 of Insulin-like growth factor-binding protein 4
Cysteine 56 of Insulin-like growth factor-binding protein 4
2dsp B 17 B 34
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 38 and 55 (17 and 34 respectively in this structure).
Details
Redox score ?
60
PDB code
2dsp
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)
7
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
38
Residue number B
55
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 38 of Insulin-like growth factor-binding protein 4
Cysteine 55 of Insulin-like growth factor-binding protein 4
2dsq B 9 B 17
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 30 and 38 (9 and 17 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
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)
7
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
30
Residue number B
38
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 30 of Insulin-like growth factor-binding protein 4
Cysteine 38 of Insulin-like growth factor-binding protein 4
1wqj B 6 B 9
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 27 and 30 (6 and 9 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
1wqj
Structure name
structural basis for the regulation of insulin-like growth factors (igfs) by igf binding proteins (igfbps)
Structure deposition date
2004-09-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
38
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
27
Residue number B
30
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 27 of Insulin-like growth factor-binding protein 4
Cysteine 30 of Insulin-like growth factor-binding protein 4
2dsr G 205 G 228
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 226 and 249 (205 and 228 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
2dsr
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 ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
226
Residue number B
249
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 226 of Insulin-like growth factor-binding protein 4
Cysteine 249 of Insulin-like growth factor-binding protein 4
1wqj B 6 B 34
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 27 and 55 (6 and 34 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
1wqj
Structure name
structural basis for the regulation of insulin-like growth factors (igfs) by igf binding proteins (igfbps)
Structure deposition date
2004-09-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
27
Residue number B
55
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 27 of Insulin-like growth factor-binding protein 4
Cysteine 55 of Insulin-like growth factor-binding protein 4
2dsr B 9 B 35
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 30 and 56 (9 and 35 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
2dsr
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 ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
30
Residue number B
56
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 30 of Insulin-like growth factor-binding protein 4
Cysteine 56 of Insulin-like growth factor-binding protein 4
2dsq A 9 A 32
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 30 and 53 (9 and 32 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
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 ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
30
Residue number B
53
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 30 of Insulin-like growth factor-binding protein 4
Cysteine 53 of Insulin-like growth factor-binding protein 4
2dsr G 194 G 228
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 215 and 249 (194 and 228 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2dsr
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 ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
215
Residue number B
249
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 215 of Insulin-like growth factor-binding protein 4
Cysteine 249 of Insulin-like growth factor-binding protein 4
2dsq B 32 B 34
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 53 and 55 (32 and 34 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
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 ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
53
Residue number B
55
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 53 of Insulin-like growth factor-binding protein 4
Cysteine 55 of Insulin-like growth factor-binding protein 4
2dsr G 205 G 207
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 226 and 228 (205 and 207 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2dsr
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 ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
226
Residue number B
228
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 226 of Insulin-like growth factor-binding protein 4
Cysteine 228 of Insulin-like growth factor-binding protein 4
2dsr G 194 G 207
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 4 between cysteines 215 and 228 (194 and 207 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
2dsr
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 ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
P22692
Residue number A
215
Residue number B
228
Peptide name
Insulin-like growth factor-binding protein 4
Ligandability
Cysteine 215 of Insulin-like growth factor-binding protein 4
Cysteine 228 of Insulin-like growth factor-binding protein 4
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