Insulin-like growth factor I
Intermolecular
Cysteine 204 of Insulin-like growth factor-binding protein 4 and cysteine 54
Cysteine 240 of Insulin-like growth factor-binding protein 3 and cysteine 54
Cysteine 96 and cysteine 206 of Insulin-like growth factor-binding protein 1
Cysteine 54 and cysteine 206 of Insulin-like growth factor-binding protein 1
Cysteine 54 and cysteine 176 of Insulin-like growth factor-binding protein 1
Cysteine 174 of Insulin-like growth factor-binding protein 4 and cysteine 54
Cysteine 204 of Insulin-like growth factor-binding protein 4 and cysteine 96
Cysteine 213 of Insulin-like growth factor-binding protein 3 and cysteine 54
Cysteine 240 of Insulin-like growth factor-binding protein 3 and cysteine 96
Cysteine 96 and cysteine 176 of Insulin-like growth factor-binding protein 1
More...Cysteine 174 of Insulin-like growth factor-binding protein 4 and cysteine 96
Cysteine 213 of Insulin-like growth factor-binding protein 3 and cysteine 96
Cysteine 40 of Insulin-like growth factor-binding protein 3 and cysteine 66
Intramolecular
Cysteine 66 and cysteine 109
Cysteine 95 and cysteine 100
Cysteine 54 and cysteine 96
Cysteine 96 and cysteine 100
Cysteine 66 and cysteine 95
Cysteine 54 and cysteine 95
Cysteine 95 and cysteine 96
Cysteine 95 and cysteine 109
Cysteine 54 and cysteine 100
Cysteine 100 and cysteine 109
Cysteine 66 and cysteine 52
Cysteine 66 and cysteine 100
Cysteine 54 and cysteine 52
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
7wrq B 213 C 6
A redox-regulated disulphide may form between cysteine 240 of Insulin-like growth factor-binding protein 3 and cysteine 54 of Insulin-like growth factor I (213 and 6 respectively in this structure).
Details
Redox score ?
63
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
5
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor-binding protein 3
Peptide B name
Insulin-like growth factor I
Peptide A accession
P17936
Peptide B accession
P05019
Peptide A residue number
240
Peptide B residue number
54
Ligandability
Cysteine 240 of Insulin-like growth factor-binding protein 3
Cysteine 54 of Insulin-like growth factor I
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
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
7wrq B 186 C 6
A redox-regulated disulphide may form between cysteine 213 of Insulin-like growth factor-binding protein 3 and cysteine 54 of Insulin-like growth factor I (186 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 ?
58
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor-binding protein 3
Peptide B name
Insulin-like growth factor I
Peptide A accession
P17936
Peptide B accession
P05019
Peptide A residue number
213
Peptide B residue number
54
Ligandability
Cysteine 213 of Insulin-like growth factor-binding protein 3
Cysteine 54 of Insulin-like growth factor I
7wrq B 213 C 48
A redox-regulated disulphide may form between cysteine 240 of Insulin-like growth factor-binding protein 3 and cysteine 96 of Insulin-like growth factor I (213 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 ?
55
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
7
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor-binding protein 3
Peptide B name
Insulin-like growth factor I
Peptide A accession
P17936
Peptide B accession
P05019
Peptide A residue number
240
Peptide B residue number
96
Ligandability
Cysteine 240 of Insulin-like growth factor-binding protein 3
Cysteine 96 of Insulin-like growth factor I
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
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
7wrq B 186 C 48
A redox-regulated disulphide may form between cysteine 213 of Insulin-like growth factor-binding protein 3 and cysteine 96 of Insulin-like growth factor I (186 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 ?
50
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor-binding protein 3
Peptide B name
Insulin-like growth factor I
Peptide A accession
P17936
Peptide B accession
P05019
Peptide A residue number
213
Peptide B residue number
96
Ligandability
Cysteine 213 of Insulin-like growth factor-binding protein 3
Cysteine 96 of Insulin-like growth factor I
7wrq B 13 C 18
A redox-regulated disulphide may form between cysteine 40 of Insulin-like growth factor-binding protein 3 and cysteine 66 of Insulin-like growth factor I (13 and 18 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
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
10
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like growth factor-binding protein 3
Peptide B name
Insulin-like growth factor I
Peptide A accession
P17936
Peptide B accession
P05019
Peptide A residue number
40
Peptide B residue number
66
Ligandability
Cysteine 40 of Insulin-like growth factor-binding protein 3
Cysteine 66 of Insulin-like growth factor I
1gzz B 18 B 61
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 66 and 109 (18 and 61 respectively in this structure).
Details
Redox score ?
87
PDB code
1gzz
Structure name
human insulin-like growth factor; hamburg data
Structure deposition date
2002-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01343
Residue number A
66
Residue number B
109
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 66 of Insulin-like growth factor I
Cysteine 109 of Insulin-like growth factor I
2dsq I 47 I 52
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 95 and 100 (47 and 52 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 ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05019
Residue number A
95
Residue number B
100
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 95 of Insulin-like growth factor I
Cysteine 100 of Insulin-like growth factor I
1gzz B 6 B 48
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 54 and 96 (6 and 48 respectively in this structure).
Details
Redox score ?
85
PDB code
1gzz
Structure name
human insulin-like growth factor; hamburg data
Structure deposition date
2002-06-10
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01343
Residue number A
54
Residue number B
96
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 54 of Insulin-like growth factor I
Cysteine 96 of Insulin-like growth factor I
6ff3 B 48 B 52
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 96 and 100 (48 and 52 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
6ff3
Structure name
crystal structure of drosophila neural ectodermal development factor imp-l1 with human igf-i
Structure deposition date
2018-01-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05019
Residue number A
96
Residue number B
100
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 96 of Insulin-like growth factor I
Cysteine 100 of Insulin-like growth factor I
3gf1 A 18 A 47
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 66 and 95 (18 and 47 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
3gf1
Structure name
solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study
Structure deposition date
1991-01-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01343
Residue number A
66
Residue number B
95
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 66 of Insulin-like growth factor I
Cysteine 95 of Insulin-like growth factor I
1tgr A 6 A 37
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 54 and 95 (6 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1tgr
Structure name
crystal structure of mini-igf-1(2)
Structure deposition date
2004-05-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01343
Residue number A
54
Residue number B
95
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 54 of Insulin-like growth factor I
Cysteine 95 of Insulin-like growth factor I
1wqj I 47 I 48
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 95 and 96 (47 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 ?
45
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)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05019
Residue number A
95
Residue number B
96
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 95 of Insulin-like growth factor I
Cysteine 96 of Insulin-like growth factor I
3gf1 A 47 A 61
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 95 and 109 (47 and 61 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
3gf1
Structure name
solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study
Structure deposition date
1991-01-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01343
Residue number A
95
Residue number B
109
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 95 of Insulin-like growth factor I
Cysteine 109 of Insulin-like growth factor I
6ff3 B 6 B 52
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 54 and 100 (6 and 52 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
6ff3
Structure name
crystal structure of drosophila neural ectodermal development factor imp-l1 with human igf-i
Structure deposition date
2018-01-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P05019
Residue number A
54
Residue number B
100
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 54 of Insulin-like growth factor I
Cysteine 100 of Insulin-like growth factor I
2gf1 A 52 A 61
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 100 and 109 (52 and 61 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
2gf1
Structure name
solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study
Structure deposition date
1991-01-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01343
Residue number A
100
Residue number B
109
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 100 of Insulin-like growth factor I
Cysteine 109 of Insulin-like growth factor I
3lri A 31 A 52
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 66 and 52 (31 and 52 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
3lri
Structure name
solution structure and backbone dynamics of long-[arg(3)]insulin-like growth factor-i
Structure deposition date
1999-04-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
nan
Peptide accession
P05019
Residue number A
66
Residue number B
52
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 66 of Insulin-like growth factor I
Cysteine 52 of Insulin-like growth factor I
Cysteine 52 in protein B could not be asigned to a Uniprot residue.
3gf1 A 18 A 52
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 66 and 100 (18 and 52 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
3gf1
Structure name
solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study
Structure deposition date
1991-01-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01343
Residue number A
66
Residue number B
100
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 66 of Insulin-like growth factor I
Cysteine 100 of Insulin-like growth factor I
3lri A 19 A 52
A redox-regulated disulphide may form within Insulin-like growth factor I between cysteines 54 and 52 (19 and 52 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
3lri
Structure name
solution structure and backbone dynamics of long-[arg(3)]insulin-like growth factor-i
Structure deposition date
1999-04-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
nan
Peptide accession
P05019
Residue number A
54
Residue number B
52
Peptide name
Insulin-like growth factor I
Ligandability
Cysteine 54 of Insulin-like growth factor I
Cysteine 52 of Insulin-like growth factor I
Cysteine 52 in protein B could not be asigned to a Uniprot residue.
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