ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Islet amyloid polypeptide

Intermolecular
Cysteine 35 and cysteine 40
Cysteine 35 and cysteine 35
Cysteine 40 and cysteine 40
Cysteine 414 of Insulin-degrading enzyme and cysteine 35
Cysteine 414 of Insulin-degrading enzyme and cysteine 40
Intramolecular
Cysteine 39 and cysteine 44
A redox-regulated disulphide may form between two units of Islet amyloid polypeptide at cysteines 35 and 40 (2 and 7 respectively in this structure).

Details

Redox score ?
82
PDB code
7yl3
Structure name
structure of hiapp-tf-type1
Structure deposition date
2022-07-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide A name
Islet amyloid polypeptide
Peptide B name
Islet amyloid polypeptide
Peptide A accession
P10997
Peptide B accession
P10997
Peptide A residue number
35
Peptide B residue number
40

Ligandability

Cysteine 35 of Islet amyloid polypeptide

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 40 of Islet amyloid polypeptide

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Islet amyloid polypeptide at cysteines 35 and 35 (2 and 2 respectively in this structure).

Details

Redox score ?
71
PDB code
7yl7
Structure name
structure of hiapp-tf-type3
Structure deposition date
2022-07-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide A name
Islet amyloid polypeptide
Peptide B name
Islet amyloid polypeptide
Peptide A accession
P10997
Peptide B accession
P10997
Peptide A residue number
35
Peptide B residue number
35

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between two units of Islet amyloid polypeptide at cysteines 40 and 40 (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 ?
45
PDB code
7yl0
Structure name
structure of hiapp-tf-type2
Structure deposition date
2022-07-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide A name
Islet amyloid polypeptide
Peptide B name
Islet amyloid polypeptide
Peptide A accession
P10997
Peptide B accession
P10997
Peptide A residue number
40
Peptide B residue number
40

Ligandability

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 414 of Insulin-degrading enzyme and cysteine 35 of Islet amyloid polypeptide (414 and 2 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
2g48
Structure name
crystal structure of human insulin-degrading enzyme in complex with amylin
Structure deposition date
2006-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
89
Peptide A name
Insulin-degrading enzyme
Peptide B name
Islet amyloid polypeptide
Peptide A accession
Q5T5N2
Peptide B accession
P10997
Peptide A residue number
414
Peptide B residue number
35

Ligandability

Cysteine 414 of Insulin-degrading enzyme

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 35 of Islet amyloid polypeptide

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form between cysteine 414 of Insulin-degrading enzyme and cysteine 40 of Islet amyloid polypeptide (414 and 2 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
2g48
Structure name
crystal structure of human insulin-degrading enzyme in complex with amylin
Structure deposition date
2006-02-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
85
Peptide A name
Insulin-degrading enzyme
Peptide B name
Islet amyloid polypeptide
Peptide A accession
Q5T5N2
Peptide B accession
P10997
Peptide A residue number
414
Peptide B residue number
40

Ligandability

Cysteine 414 of Insulin-degrading enzyme

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 40 of Islet amyloid polypeptide

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Islet amyloid polypeptide between cysteines 39 and 44 (2 and 7 respectively in this structure).

Details

Redox score ?
87
PDB code
2kj7
Structure name
three-dimensional nmr structure of rat islet amyloid polypeptide in dpc micelles
Structure deposition date
2009-05-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
21
Minimum pKa ?
nan
% buried
nan
Peptide accession
P12969
Residue number A
39
Residue number B
44
Peptide name
Islet amyloid polypeptide

Ligandability

Cysteine 39 of Islet amyloid polypeptide

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 44 of Islet amyloid polypeptide

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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