Insulin
Intermolecular
Cysteine 83 and cysteine 31
Cysteine 88 and cysteine 31
Cysteine 31 and cysteine 31
Cysteine 84 and cysteine 31
Intramolecular
Cysteine 43 and cysteine 97
Cysteine 83 and cysteine 88
Cysteine 84 and cysteine 88
Cysteine 83 and cysteine 84
Cysteine 83 and cysteine 97
2w44 C 6 D 7
A redox-regulated disulphide may form between two units of Insulin at cysteines 83 and 31 (6 and 7 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
2w44
Structure name
structure deltaa1-a4 insulin
Structure deposition date
2008-11-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
A6XGL2
Peptide B accession
A6XGL2
Peptide A residue number
83
Peptide B residue number
31
Ligandability
Cysteine 83 of Insulin
Cysteine 31 of Insulin
2w44 E 11 F 7
A redox-regulated disulphide may form between two units of Insulin at cysteines 88 and 31 (11 and 7 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
2w44
Structure name
structure deltaa1-a4 insulin
Structure deposition date
2008-11-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
A6XGL2
Peptide B accession
A6XGL2
Peptide A residue number
88
Peptide B residue number
31
Ligandability
Cysteine 88 of Insulin
Cysteine 31 of Insulin
5wdm A 7 C 7
A redox-regulated disulphide may form between two units of Insulin at cysteines 31 and 31 (7 and 7 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
5wdm
Structure name
an ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein
Structure deposition date
2017-07-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
A6XGL2
Peptide B accession
A6XGL2
Peptide A residue number
31
Peptide B residue number
31
Ligandability
5wdm A 43 C 7
A redox-regulated disulphide may form between two units of Insulin at cysteines 84 and 31 (43 and 7 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
5wdm
Structure name
an ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein
Structure deposition date
2017-07-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
A6XGL2
Peptide B accession
A6XGL2
Peptide A residue number
84
Peptide B residue number
31
Ligandability
Cysteine 84 of Insulin
Cysteine 31 of Insulin
5wdm E 19 E 56
A redox-regulated disulphide may form within Insulin between cysteines 43 and 97 (19 and 56 respectively in this structure).
Details
Redox score ?
88
PDB code
5wdm
Structure name
an ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein
Structure deposition date
2017-07-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6XGL2
Residue number A
43
Residue number B
97
Peptide name
Insulin
Ligandability
Cysteine 43 of Insulin
Cysteine 97 of Insulin
5wdm D 42 D 47
A redox-regulated disulphide may form within Insulin between cysteines 83 and 88 (42 and 47 respectively in this structure).
Details
Redox score ?
87
PDB code
5wdm
Structure name
an ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein
Structure deposition date
2017-07-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6XGL2
Residue number A
83
Residue number B
88
Peptide name
Insulin
Ligandability
Cysteine 83 of Insulin
Cysteine 88 of Insulin
2w44 A 7 A 11
A redox-regulated disulphide may form within Insulin between cysteines 84 and 88 (7 and 11 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
2w44
Structure name
structure deltaa1-a4 insulin
Structure deposition date
2008-11-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6XGL2
Residue number A
84
Residue number B
88
Peptide name
Insulin
Ligandability
Cysteine 84 of Insulin
Cysteine 88 of Insulin
5wdm F 42 F 43
A redox-regulated disulphide may form within Insulin between cysteines 83 and 84 (42 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 ?
47
PDB code
5wdm
Structure name
an ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein
Structure deposition date
2017-07-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6XGL2
Residue number A
83
Residue number B
84
Peptide name
Insulin
Ligandability
Cysteine 83 of Insulin
Cysteine 84 of Insulin
5wdm B 42 B 56
A redox-regulated disulphide may form within Insulin between cysteines 83 and 97 (42 and 56 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
5wdm
Structure name
an ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein
Structure deposition date
2017-07-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
A6XGL2
Residue number A
83
Residue number B
97
Peptide name
Insulin
Ligandability
Cysteine 83 of Insulin
Cysteine 97 of Insulin
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