Insulin-like growth factor-binding protein 6
Intramolecular
Cysteine 40 and cysteine 44
Cysteine 57 and cysteine 63
Cysteine 29 and cysteine 32
Cysteine 201 and cysteine 212
Cysteine 163 and cysteine 190
Cysteine 214 and cysteine 234
Cysteine 201 and cysteine 214
Cysteine 212 and cysteine 214
Cysteine 201 and cysteine 234
Cysteine 163 and cysteine 212
More...Cysteine 212 and cysteine 234
Cysteine 190 and cysteine 212
Cysteine 163 and cysteine 201
Cysteine 190 and cysteine 201
2jm2 A 16 A 20
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 40 and 44 (16 and 20 respectively in this structure).
Details
Redox score ?
88
PDB code
2jm2
Structure name
structure of the n-terminal subdomain of insulin-like growth factor (igf) binding protein-6 and its interactions with igfs
Structure deposition date
2006-09-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
27
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
40
Residue number B
44
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 40 of Insulin-like growth factor-binding protein 6
Cysteine 44 of Insulin-like growth factor-binding protein 6
2jm2 A 33 A 39
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 57 and 63 (33 and 39 respectively in this structure).
Details
Redox score ?
88
PDB code
2jm2
Structure name
structure of the n-terminal subdomain of insulin-like growth factor (igf) binding protein-6 and its interactions with igfs
Structure deposition date
2006-09-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
29
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
57
Residue number B
63
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 57 of Insulin-like growth factor-binding protein 6
Cysteine 63 of Insulin-like growth factor-binding protein 6
2jm2 A 5 A 8
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 29 and 32 (5 and 8 respectively in this structure).
Details
Redox score ?
87
PDB code
2jm2
Structure name
structure of the n-terminal subdomain of insulin-like growth factor (igf) binding protein-6 and its interactions with igfs
Structure deposition date
2006-09-18
Thiol separation (Å)
2
Half-sphere exposure sum ?
23
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
29
Residue number B
32
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 29 of Insulin-like growth factor-binding protein 6
Cysteine 32 of Insulin-like growth factor-binding protein 6
1rmj A 41 A 52
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 201 and 212 (41 and 52 respectively in this structure).
Details
Redox score ?
86
PDB code
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
201
Residue number B
212
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 201 of Insulin-like growth factor-binding protein 6
Cysteine 212 of Insulin-like growth factor-binding protein 6
1rmj A 3 A 30
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 163 and 190 (3 and 30 respectively in this structure).
Details
Redox score ?
84
PDB code
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
163
Residue number B
190
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 163 of Insulin-like growth factor-binding protein 6
Cysteine 190 of Insulin-like growth factor-binding protein 6
1rmj A 54 A 74
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 214 and 234 (54 and 74 respectively in this structure).
Details
Redox score ?
83
PDB code
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
2
Half-sphere exposure sum ?
67
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
214
Residue number B
234
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 214 of Insulin-like growth factor-binding protein 6
Cysteine 234 of Insulin-like growth factor-binding protein 6
1rmj A 41 A 54
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 201 and 214 (41 and 54 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
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
201
Residue number B
214
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 201 of Insulin-like growth factor-binding protein 6
Cysteine 214 of Insulin-like growth factor-binding protein 6
1rmj A 52 A 54
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 212 and 214 (52 and 54 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
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
212
Residue number B
214
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 212 of Insulin-like growth factor-binding protein 6
Cysteine 214 of Insulin-like growth factor-binding protein 6
1rmj A 41 A 74
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 201 and 234 (41 and 74 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
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
201
Residue number B
234
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 201 of Insulin-like growth factor-binding protein 6
Cysteine 234 of Insulin-like growth factor-binding protein 6
1rmj A 3 A 52
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 163 and 212 (3 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
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
163
Residue number B
212
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 163 of Insulin-like growth factor-binding protein 6
Cysteine 212 of Insulin-like growth factor-binding protein 6
1rmj A 52 A 74
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 212 and 234 (52 and 74 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
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
212
Residue number B
234
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 212 of Insulin-like growth factor-binding protein 6
Cysteine 234 of Insulin-like growth factor-binding protein 6
1rmj A 30 A 52
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 190 and 212 (30 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 ?
41
PDB code
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
190
Residue number B
212
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 190 of Insulin-like growth factor-binding protein 6
Cysteine 212 of Insulin-like growth factor-binding protein 6
1rmj A 3 A 41
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 163 and 201 (3 and 41 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
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
163
Residue number B
201
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 163 of Insulin-like growth factor-binding protein 6
Cysteine 201 of Insulin-like growth factor-binding protein 6
1rmj A 30 A 41
A redox-regulated disulphide may form within Insulin-like growth factor-binding protein 6 between cysteines 190 and 201 (30 and 41 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
1rmj
Structure name
c-terminal domain of insulin-like growth factor (igf) binding protein- 6: structure and interaction with igf-ii
Structure deposition date
2003-11-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P24592
Residue number A
190
Residue number B
201
Peptide name
Insulin-like growth factor-binding protein 6
Ligandability
Cysteine 190 of Insulin-like growth factor-binding protein 6
Cysteine 201 of Insulin-like growth factor-binding protein 6
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