Insulin
Intermolecular
Cysteine 109 and cysteine 43
Cysteine 96 and cysteine 31 of Insulin, isoform 2
Cysteine 43 of Insulin, isoform 2 and cysteine 109
Cysteine 109 and cysteine 22
Cysteine 100 and cysteine 31 of Insulin, isoform 2
Cysteine 96 and cysteine 96
Cysteine 95 and cysteine 31 of Insulin, isoform 2
Cysteine 100 and cysteine 31
Cysteine 95 and cysteine 43
Cysteine 100 and cysteine 43
More...Cysteine 31 and cysteine 31
Cysteine 95 and cysteine 31
Intramolecular
Cysteine 94 and cysteine 94
Cysteine 31 and cysteine 94
Cysteine 31 and cysteine 31
Cysteine 43 and cysteine 107
Cysteine 19 and cysteine 109
Cysteine 95 and cysteine 100
Cysteine 109 and cysteine 109
Cysteine 43 and cysteine 22
Cysteine 31 and cysteine 98
Cysteine 95 and cysteine 96
Cysteine 96 and cysteine 100
Cysteine 31 and cysteine 95
Cysteine 95 and cysteine 109
Cysteine 43 and cysteine 25
Cysteine 31 and cysteine 43
Cysteine 100 and cysteine 109
2hh4 A 20 B 19
A redox-regulated disulphide may form between two units of Insulin at cysteines 109 and 43 (20 and 19 respectively in this structure).
Details
Redox score ?
88
PDB code
2hh4
Structure name
nmr structure of human insulin mutant gly-b8-d-ser, his-b10-asp pro- b28-lys, lys-b29-pro, 20 structures
Structure deposition date
2006-06-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
Q5EEX2
Peptide B accession
Q5EEX2
Peptide A residue number
109
Peptide B residue number
43
Ligandability
Cysteine 109 of Insulin
Cysteine 43 of Insulin
8guy C 7 D 7
A redox-regulated disulphide may form between cysteine 96 of Insulin and cysteine 31 of Insulin, isoform 2 (7 and 7 respectively in this structure).
Details
Redox score ?
86
PDB code
8guy
Structure name
human insulin receptor bound with two insulin molecules
Structure deposition date
2022-09-14
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin, isoform 2
Peptide A accession
P01308
Peptide B accession
F8WCM5
Peptide A residue number
96
Peptide B residue number
31
Ligandability
Cysteine 96 of Insulin
Cysteine 31 of Insulin, isoform 2
7yq4 B 19 A 20
A redox-regulated disulphide may form between cysteine 43 of Insulin, isoform 2 and cysteine 109 of Insulin (19 and 20 respectively in this structure).
Details
Redox score ?
85
PDB code
7yq4
Structure name
human insulin receptor bound with a62 dna aptamer and insulin - locally refined
Structure deposition date
2022-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin, isoform 2
Peptide B name
Insulin
Peptide A accession
F8WCM5
Peptide B accession
P01308
Peptide A residue number
43
Peptide B residue number
109
Ligandability
Cysteine 43 of Insulin, isoform 2
Cysteine 109 of Insulin
6tyh E 20 F 22
A redox-regulated disulphide may form between two units of Insulin at cysteines 109 and 22 (20 and 22 respectively in this structure).
Details
Redox score ?
62
PDB code
6tyh
Structure name
four-disulfide insulin analog a22/b22
Structure deposition date
2019-08-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
P01308
Peptide B accession
P01308
Peptide A residue number
109
Peptide B residue number
22
Ligandability
Cysteine 109 of Insulin
Cysteine 22 of Insulin
Cysteine 22 in protein B could not be asigned to a Uniprot residue.
7yq3 A 11 B 7
A redox-regulated disulphide may form between cysteine 100 of Insulin and cysteine 31 of Insulin, isoform 2 (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 ?
53
PDB code
7yq3
Structure name
human insulin receptor bound with a43 dna aptamer and insulin
Structure deposition date
2022-08-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin, isoform 2
Peptide A accession
P01308
Peptide B accession
F8WCM5
Peptide A residue number
100
Peptide B residue number
31
Ligandability
Cysteine 100 of Insulin
Cysteine 31 of Insulin, isoform 2
3w80 C 7 E 7
A redox-regulated disulphide may form between two units of Insulin at cysteines 96 and 96 (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 ?
50
PDB code
3w80
Structure name
crystal structure of dodecamer human insulin with double c-axis length of the hexamer 2 zn insulin cell
Structure deposition date
2013-03-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
P01308
Peptide B accession
P01308
Peptide A residue number
96
Peptide B residue number
96
Ligandability
7yq3 A 6 B 7
A redox-regulated disulphide may form between cysteine 95 of Insulin and cysteine 31 of Insulin, isoform 2 (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 ?
50
PDB code
7yq3
Structure name
human insulin receptor bound with a43 dna aptamer and insulin
Structure deposition date
2022-08-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin, isoform 2
Peptide A accession
P01308
Peptide B accession
F8WCM5
Peptide A residue number
95
Peptide B residue number
31
Ligandability
Cysteine 95 of Insulin
Cysteine 31 of Insulin, isoform 2
3ilg A 11 B 7
A redox-regulated disulphide may form between two units of Insulin at cysteines 100 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 ?
43
PDB code
3ilg
Structure name
crystal structure of humnan insulin sr+2 complex
Structure deposition date
2009-08-07
Thiol separation (Å)
9
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
P01308
Peptide B accession
P01308
Peptide A residue number
100
Peptide B residue number
31
Ligandability
Cysteine 100 of Insulin
Cysteine 31 of Insulin
3zs2 C 6 D 19
A redox-regulated disulphide may form between two units of Insulin at cysteines 95 and 43 (6 and 19 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
3zs2
Structure name
tyrb25,nmepheb26,lysb28,prob29-insulin analogue crystal structure
Structure deposition date
2011-06-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
P01308
Peptide B accession
P01308
Peptide A residue number
95
Peptide B residue number
43
Ligandability
Cysteine 95 of Insulin
Cysteine 43 of Insulin
1hiq A 11 B 19
A redox-regulated disulphide may form between two units of Insulin at cysteines 100 and 43 (11 and 19 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
1hiq
Structure name
paradoxical structure and function in a mutant human insulin associated with diabetes mellitus
Structure deposition date
1993-03-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
P01308
Peptide B accession
P01308
Peptide A residue number
100
Peptide B residue number
43
Ligandability
Cysteine 100 of Insulin
Cysteine 43 of Insulin
3w80 D 7 F 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 ?
39
PDB code
3w80
Structure name
crystal structure of dodecamer human insulin with double c-axis length of the hexamer 2 zn insulin cell
Structure deposition date
2013-03-11
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
P01308
Peptide B accession
P01308
Peptide A residue number
31
Peptide B residue number
31
Ligandability
6ce9 N 6 O 7
A redox-regulated disulphide may form between two units of Insulin at cysteines 95 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 ?
31
PDB code
6ce9
Structure name
insulin receptor ectodomain in complex with two insulin molecules
Structure deposition date
2018-02-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
16
% buried
nan
Peptide A name
Insulin
Peptide B name
Insulin
Peptide A accession
P01308
Peptide B accession
P01318
Peptide A residue number
95
Peptide B residue number
31
Ligandability
Cysteine 95 of Insulin
Cysteine 31 of Insulin
6ins E 7 E 7
A redox-regulated disulphide may form within Insulin between cysteines 94 and 94 (7 and 7 respectively in this structure).
Details
Redox score ?
95
PDB code
6ins
Structure name
x-ray analysis of the single chain b29-a1 peptide-linked insulin molecule
Structure deposition date
1992-11-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01315
Residue number A
94
Residue number B
94
Peptide name
Insulin
Ligandability
6ins E 7 E 7
A redox-regulated disulphide may form within Insulin between cysteines 31 and 94 (7 and 7 respectively in this structure).
Details
Redox score ?
95
PDB code
6ins
Structure name
x-ray analysis of the single chain b29-a1 peptide-linked insulin molecule
Structure deposition date
1992-11-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01315
Residue number A
31
Residue number B
94
Peptide name
Insulin
Ligandability
Cysteine 31 of Insulin
Cysteine 94 of Insulin
6ins E 7 E 7
A redox-regulated disulphide may form within Insulin between cysteines 31 and 31 (7 and 7 respectively in this structure).
Details
Redox score ?
95
PDB code
6ins
Structure name
x-ray analysis of the single chain b29-a1 peptide-linked insulin molecule
Structure deposition date
1992-11-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01315
Residue number A
31
Residue number B
31
Peptide name
Insulin
Ligandability
6ins F 19 F 20
A redox-regulated disulphide may form within Insulin between cysteines 43 and 107 (19 and 20 respectively in this structure).
Details
Redox score ?
94
PDB code
6ins
Structure name
x-ray analysis of the single chain b29-a1 peptide-linked insulin molecule
Structure deposition date
1992-11-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01315
Residue number A
43
Residue number B
107
Peptide name
Insulin
Ligandability
Cysteine 43 of Insulin
Cysteine 107 of Insulin
6b3q a 19 a 195
A redox-regulated disulphide may form within Insulin between cysteines 19 and 109 (19 and 195 respectively in this structure).
Details
Redox score ?
91
PDB code
6b3q
Structure name
cryo-em structure of human insulin degrading enzyme in complex with insulin
Structure deposition date
2017-09-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01308
Residue number A
19
Residue number B
109
Peptide name
Insulin
Ligandability
Cysteine 19 of Insulin
Cysteine 109 of Insulin
Cysteine 19 in protein A could not be asigned to a Uniprot residue.
2hh4 A 6 A 11
A redox-regulated disulphide may form within Insulin between cysteines 95 and 100 (6 and 11 respectively in this structure).
Details
Redox score ?
88
PDB code
2hh4
Structure name
nmr structure of human insulin mutant gly-b8-d-ser, his-b10-asp pro- b28-lys, lys-b29-pro, 20 structures
Structure deposition date
2006-06-27
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EEX2
Residue number A
95
Residue number B
100
Peptide name
Insulin
Ligandability
Cysteine 95 of Insulin
Cysteine 100 of Insulin
6tyh C 20 C 22
A redox-regulated disulphide may form within Insulin between cysteines 109 and 109 (20 and 22 respectively in this structure).
Details
Redox score ?
72
PDB code
6tyh
Structure name
four-disulfide insulin analog a22/b22
Structure deposition date
2019-08-08
Thiol separation (Å)
5
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01308
Residue number A
109
Residue number B
109
Peptide name
Insulin
Ligandability
Cysteine 109 of Insulin
Cysteine 109 of Insulin
6tyh H 19 H 22
A redox-regulated disulphide may form within Insulin between cysteines 43 and 22 (19 and 22 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
6tyh
Structure name
four-disulfide insulin analog a22/b22
Structure deposition date
2019-08-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01308
Residue number A
43
Residue number B
22
Peptide name
Insulin
Ligandability
Cysteine 43 of Insulin
Cysteine 22 of Insulin
Cysteine 22 in protein B could not be asigned to a Uniprot residue.
6ins E 7 E 11
A redox-regulated disulphide may form within Insulin between cysteines 31 and 98 (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 ?
56
PDB code
6ins
Structure name
x-ray analysis of the single chain b29-a1 peptide-linked insulin molecule
Structure deposition date
1992-11-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01315
Residue number A
31
Residue number B
98
Peptide name
Insulin
Ligandability
Cysteine 31 of Insulin
Cysteine 98 of Insulin
2hh4 A 6 A 7
A redox-regulated disulphide may form within Insulin between cysteines 95 and 96 (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
2hh4
Structure name
nmr structure of human insulin mutant gly-b8-d-ser, his-b10-asp pro- b28-lys, lys-b29-pro, 20 structures
Structure deposition date
2006-06-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EEX2
Residue number A
95
Residue number B
96
Peptide name
Insulin
Ligandability
Cysteine 95 of Insulin
Cysteine 96 of Insulin
4xc4 A 7 A 11
A redox-regulated disulphide may form within Insulin between cysteines 96 and 100 (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 ?
47
PDB code
4xc4
Structure name
insulin co-crystallizes in the presence of it beta-cell chaperone sulfatide
Structure deposition date
2014-12-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01308
Residue number A
96
Residue number B
100
Peptide name
Insulin
Ligandability
Cysteine 96 of Insulin
Cysteine 100 of Insulin
7jp3 F 7 F 34
A redox-regulated disulphide may form within Insulin between cysteines 31 and 95 (7 and 34 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
7jp3
Structure name
des-b29,b30-insulin
Structure deposition date
2020-08-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01308
Residue number A
31
Residue number B
95
Peptide name
Insulin
Ligandability
Cysteine 31 of Insulin
Cysteine 95 of Insulin
2n2w A 6 A 20
A redox-regulated disulphide may form within Insulin between cysteines 95 and 109 (6 and 20 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
2n2w
Structure name
solution structure of [b26-b29 triazole cross-linked]-insulin analogue at ph 8
Structure deposition date
2015-05-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01308
Residue number A
95
Residue number B
109
Peptide name
Insulin
Ligandability
Cysteine 95 of Insulin
Cysteine 109 of Insulin
3u4n B 19 B 25
A redox-regulated disulphide may form within Insulin between cysteines 43 and 25 (19 and 25 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
3u4n
Structure name
a novel covalently linked insulin dimer
Structure deposition date
2011-10-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
nan
Peptide accession
P01308
Residue number A
43
Residue number B
25
Peptide name
Insulin
Ligandability
Cysteine 43 of Insulin
Cysteine 25 of Insulin
Cysteine 25 in protein B could not be asigned to a Uniprot residue.
6bfc b 7 b 19
A redox-regulated disulphide may form within Insulin between cysteines 31 and 43 (7 and 19 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
6bfc
Structure name
cryo-em structure of human insulin degrading enzyme in complex with insulin
Structure deposition date
2017-10-26
Thiol separation (Å)
10
Half-sphere exposure sum ?
nan
Minimum pKa ?
9
% buried
nan
Peptide accession
P01308
Residue number A
31
Residue number B
43
Peptide name
Insulin
Ligandability
Cysteine 31 of Insulin
Cysteine 43 of Insulin
1mhi A 11 A 20
A redox-regulated disulphide may form within Insulin between cysteines 100 and 109 (11 and 20 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
1mhi
Structure name
three-dimensional solution structure of an insulin dimer
Structure deposition date
1994-11-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P01308
Residue number A
100
Residue number B
109
Peptide name
Insulin
Ligandability
Cysteine 100 of Insulin
Cysteine 109 of Insulin
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