Insulin-like growth factor-binding protein 3
Intermolecular
Cysteine 240 and cysteine 54 of Insulin-like growth factor I
Cysteine 213 and cysteine 54 of Insulin-like growth factor I
Cysteine 240 and cysteine 96 of Insulin-like growth factor I
Cysteine 213 and cysteine 96 of Insulin-like growth factor I
Cysteine 40 and cysteine 66 of Insulin-like growth factor I
Intramolecular
Cysteine 51 and cysteine 70
Cysteine 43 and cysteine 69
Cysteine 58 and cysteine 73
Cysteine 81 and cysteine 94
Cysteine 88 and cysteine 114
More...Cysteine 264 and cysteine 285
Cysteine 213 and cysteine 240
Cysteine 251 and cysteine 262
Cysteine 40 and cysteine 67
Cysteine 81 and cysteine 88
Cysteine 81 and cysteine 114
Cysteine 88 and cysteine 94
Cysteine 94 and cysteine 114
Cysteine 69 and cysteine 70
Cysteine 51 and cysteine 69
Cysteine 43 and cysteine 70
Cysteine 251 and cysteine 285
Cysteine 262 and cysteine 285
Cysteine 43 and cysteine 51
Cysteine 43 and cysteine 67
Cysteine 262 and cysteine 264
Cysteine 251 and cysteine 264
Cysteine 67 and cysteine 69
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
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
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
7wrq B 24 B 43
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 51 and 70 (24 and 43 respectively in this structure).
Details
Redox score ?
86
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
51
Residue number B
70
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 51 of Insulin-like growth factor-binding protein 3
Cysteine 70 of Insulin-like growth factor-binding protein 3
7wrq B 16 B 42
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 43 and 69 (16 and 42 respectively in this structure).
Details
Redox score ?
86
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
43
Residue number B
69
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 43 of Insulin-like growth factor-binding protein 3
Cysteine 69 of Insulin-like growth factor-binding protein 3
7wrq B 31 B 46
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 58 and 73 (31 and 46 respectively in this structure).
Details
Redox score ?
85
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
58
Residue number B
73
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 58 of Insulin-like growth factor-binding protein 3
Cysteine 73 of Insulin-like growth factor-binding protein 3
7wrq B 54 B 67
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 81 and 94 (54 and 67 respectively in this structure).
Details
Redox score ?
85
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
81
Residue number B
94
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 81 of Insulin-like growth factor-binding protein 3
Cysteine 94 of Insulin-like growth factor-binding protein 3
7wrq B 61 B 87
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 88 and 114 (61 and 87 respectively in this structure).
Details
Redox score ?
85
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
88
Residue number B
114
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 88 of Insulin-like growth factor-binding protein 3
Cysteine 114 of Insulin-like growth factor-binding protein 3
7wrq B 237 B 258
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 264 and 285 (237 and 258 respectively in this structure).
Details
Redox score ?
84
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
264
Residue number B
285
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 264 of Insulin-like growth factor-binding protein 3
Cysteine 285 of Insulin-like growth factor-binding protein 3
7wrq B 186 B 213
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 213 and 240 (186 and 213 respectively in this structure).
Details
Redox score ?
84
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
213
Residue number B
240
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 213 of Insulin-like growth factor-binding protein 3
Cysteine 240 of Insulin-like growth factor-binding protein 3
7wrq B 224 B 235
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 251 and 262 (224 and 235 respectively in this structure).
Details
Redox score ?
83
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
251
Residue number B
262
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 251 of Insulin-like growth factor-binding protein 3
Cysteine 262 of Insulin-like growth factor-binding protein 3
7wrq B 13 B 40
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 40 and 67 (13 and 40 respectively in this structure).
Details
Redox score ?
82
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
40
Residue number B
67
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 40 of Insulin-like growth factor-binding protein 3
Cysteine 67 of Insulin-like growth factor-binding protein 3
7wrq B 54 B 61
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 81 and 88 (54 and 61 respectively in this structure).
Details
Redox score ?
75
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
81
Residue number B
88
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 81 of Insulin-like growth factor-binding protein 3
Cysteine 88 of Insulin-like growth factor-binding protein 3
7wrq B 54 B 87
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 81 and 114 (54 and 87 respectively in this structure).
Details
Redox score ?
74
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
81
Residue number B
114
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 81 of Insulin-like growth factor-binding protein 3
Cysteine 114 of Insulin-like growth factor-binding protein 3
7wrq B 61 B 67
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 88 and 94 (61 and 67 respectively in this structure).
Details
Redox score ?
71
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
88
Residue number B
94
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 88 of Insulin-like growth factor-binding protein 3
Cysteine 94 of Insulin-like growth factor-binding protein 3
7wrq B 67 B 87
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 94 and 114 (67 and 87 respectively in this structure).
Details
Redox score ?
69
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 ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
94
Residue number B
114
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 94 of Insulin-like growth factor-binding protein 3
Cysteine 114 of Insulin-like growth factor-binding protein 3
7wrq B 42 B 43
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 69 and 70 (42 and 43 respectively in this structure).
Details
Redox score ?
61
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
69
Residue number B
70
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 69 of Insulin-like growth factor-binding protein 3
Cysteine 70 of Insulin-like growth factor-binding protein 3
7wrq B 24 B 42
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 51 and 69 (24 and 42 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
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 ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
51
Residue number B
69
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 51 of Insulin-like growth factor-binding protein 3
Cysteine 69 of Insulin-like growth factor-binding protein 3
7wrq B 16 B 43
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 43 and 70 (16 and 43 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)
8
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
43
Residue number B
70
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 43 of Insulin-like growth factor-binding protein 3
Cysteine 70 of Insulin-like growth factor-binding protein 3
7wrq B 224 B 258
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 251 and 285 (224 and 258 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
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 ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
251
Residue number B
285
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 251 of Insulin-like growth factor-binding protein 3
Cysteine 285 of Insulin-like growth factor-binding protein 3
7wrq B 235 B 258
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 262 and 285 (235 and 258 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
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 ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
262
Residue number B
285
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 262 of Insulin-like growth factor-binding protein 3
Cysteine 285 of Insulin-like growth factor-binding protein 3
7wrq B 16 B 24
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 43 and 51 (16 and 24 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
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
37
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
43
Residue number B
51
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 43 of Insulin-like growth factor-binding protein 3
Cysteine 51 of Insulin-like growth factor-binding protein 3
7wrq B 16 B 40
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 43 and 67 (16 and 40 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
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 ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
43
Residue number B
67
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 43 of Insulin-like growth factor-binding protein 3
Cysteine 67 of Insulin-like growth factor-binding protein 3
7wrq B 235 B 237
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 262 and 264 (235 and 237 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
262
Residue number B
264
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 262 of Insulin-like growth factor-binding protein 3
Cysteine 264 of Insulin-like growth factor-binding protein 3
7wrq B 224 B 237
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 251 and 264 (224 and 237 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
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
251
Residue number B
264
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 251 of Insulin-like growth factor-binding protein 3
Cysteine 264 of Insulin-like growth factor-binding protein 3
7wrq B 40 B 42
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 3 between cysteines 67 and 69 (40 and 42 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
7wrq
Structure name
structure of human igf1/igfbp3/als ternary complex
Structure deposition date
2022-01-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P17936
Residue number A
67
Residue number B
69
Peptide name
Insulin-like growth factor-binding protein 3
Ligandability
Cysteine 67 of Insulin-like growth factor-binding protein 3
Cysteine 69 of Insulin-like growth factor-binding protein 3
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