Insulin-like 3
Intermolecular
Cysteine 129 and cysteine 46
Cysteine 116 and cysteine 34
Cysteine 46 and cysteine 120
Cysteine 115 and cysteine 34
Cysteine 115 and cysteine 46
Cysteine 120 and cysteine 34
Intramolecular
Cysteine 115 and cysteine 120
Cysteine 115 and cysteine 116
Cysteine 120 and cysteine 129
Cysteine 115 and cysteine 129
Cysteine 116 and cysteine 120
2k6t A 129 B 46
A redox-regulated disulphide may form between two units of Insulin-like 3 at cysteines 129 and 46.
Details
Redox score ?
86
PDB code
2k6t
Structure name
solution structure of the relaxin-like factor
Structure deposition date
2008-07-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like 3
Peptide B name
Insulin-like 3
Peptide A accession
P51460
Peptide B accession
P51460
Peptide A residue number
129
Peptide B residue number
46
Ligandability
Cysteine 129 of Insulin-like 3
Cysteine 46 of Insulin-like 3
2k6t A 116 B 34
A redox-regulated disulphide may form between two units of Insulin-like 3 at cysteines 116 and 34.
Details
Redox score ?
82
PDB code
2k6t
Structure name
solution structure of the relaxin-like factor
Structure deposition date
2008-07-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
45
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like 3
Peptide B name
Insulin-like 3
Peptide A accession
P51460
Peptide B accession
P51460
Peptide A residue number
116
Peptide B residue number
34
Ligandability
Cysteine 116 of Insulin-like 3
Cysteine 34 of Insulin-like 3
2h8b B 22 A 15
A redox-regulated disulphide may form between two units of Insulin-like 3 at cysteines 46 and 120 (22 and 15 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
2h8b
Structure name
solution structure of insl3
Structure deposition date
2006-06-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like 3
Peptide B name
Insulin-like 3
Peptide A accession
P51460
Peptide B accession
P51460
Peptide A residue number
46
Peptide B residue number
120
Ligandability
Cysteine 46 of Insulin-like 3
Cysteine 120 of Insulin-like 3
2k6u A 115 B 34
A redox-regulated disulphide may form between two units of Insulin-like 3 at cysteines 115 and 34. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2k6u
Structure name
the solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor (rlf)
Structure deposition date
2008-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like 3
Peptide B name
Insulin-like 3
Peptide A accession
P51460
Peptide B accession
P51460
Peptide A residue number
115
Peptide B residue number
34
Ligandability
Cysteine 115 of Insulin-like 3
Cysteine 34 of Insulin-like 3
2k6u A 115 B 46
A redox-regulated disulphide may form between two units of Insulin-like 3 at cysteines 115 and 46. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2k6u
Structure name
the solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor (rlf)
Structure deposition date
2008-07-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like 3
Peptide B name
Insulin-like 3
Peptide A accession
P51460
Peptide B accession
P51460
Peptide A residue number
115
Peptide B residue number
46
Ligandability
Cysteine 115 of Insulin-like 3
Cysteine 46 of Insulin-like 3
2k6u A 120 B 34
A redox-regulated disulphide may form between two units of Insulin-like 3 at cysteines 120 and 34. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
2k6u
Structure name
the solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor (rlf)
Structure deposition date
2008-07-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin-like 3
Peptide B name
Insulin-like 3
Peptide A accession
P51460
Peptide B accession
P51460
Peptide A residue number
120
Peptide B residue number
34
Ligandability
Cysteine 120 of Insulin-like 3
Cysteine 34 of Insulin-like 3
2h8b A 10 A 15
A redox-regulated disulphide may form within Insulin-like 3 between cysteines 115 and 120 (10 and 15 respectively in this structure).
Details
Redox score ?
86
PDB code
2h8b
Structure name
solution structure of insl3
Structure deposition date
2006-06-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P51460
Residue number A
115
Residue number B
120
Peptide name
Insulin-like 3
Ligandability
Cysteine 115 of Insulin-like 3
Cysteine 120 of Insulin-like 3
2k6t A 115 A 116
A redox-regulated disulphide may form within Insulin-like 3 between cysteines 115 and 116. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
2k6t
Structure name
solution structure of the relaxin-like factor
Structure deposition date
2008-07-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
P51460
Residue number A
115
Residue number B
116
Peptide name
Insulin-like 3
Ligandability
Cysteine 115 of Insulin-like 3
Cysteine 116 of Insulin-like 3
2h8b A 15 A 24
A redox-regulated disulphide may form within Insulin-like 3 between cysteines 120 and 129 (15 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 ?
44
PDB code
2h8b
Structure name
solution structure of insl3
Structure deposition date
2006-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P51460
Residue number A
120
Residue number B
129
Peptide name
Insulin-like 3
Ligandability
Cysteine 120 of Insulin-like 3
Cysteine 129 of Insulin-like 3
2h8b A 10 A 24
A redox-regulated disulphide may form within Insulin-like 3 between cysteines 115 and 129 (10 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 ?
43
PDB code
2h8b
Structure name
solution structure of insl3
Structure deposition date
2006-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P51460
Residue number A
115
Residue number B
129
Peptide name
Insulin-like 3
Ligandability
Cysteine 115 of Insulin-like 3
Cysteine 129 of Insulin-like 3
2h8b A 11 A 15
A redox-regulated disulphide may form within Insulin-like 3 between cysteines 116 and 120 (11 and 15 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
2h8b
Structure name
solution structure of insl3
Structure deposition date
2006-06-07
Thiol separation (Å)
10
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P51460
Residue number A
116
Residue number B
120
Peptide name
Insulin-like 3
Ligandability
Cysteine 116 of Insulin-like 3
Cysteine 120 of Insulin-like 3
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