ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Insulin-degrading enzyme

Intermolecular
Cysteine 414 and cysteine 35 of Islet amyloid polypeptide
Cysteine 414 and cysteine 40 of Islet amyloid polypeptide
Intramolecular
Cysteine 573 and cysteine 904
Cysteine 789 and cysteine 966
Cysteine 812 and cysteine 819
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 Insulin-degrading enzyme between cysteines 573 and 904.

Details

Redox score ?
69
PDB code
2jg4
Structure name
substrate-free ide structure in its closed conformation
Structure deposition date
2007-02-07
Thiol separation (Å)
4
Half-sphere exposure sum ?
81
Minimum pKa ?
8
% buried
96
Peptide accession
P14735
Residue number A
573
Residue number B
904
Peptide name
Insulin-degrading enzyme

Ligandability

Cysteine 573 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 904 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.

A redox-regulated disulphide may form within Insulin-degrading enzyme between cysteines 789 and 966. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
55
PDB code
2jg4
Structure name
substrate-free ide structure in its closed conformation
Structure deposition date
2007-02-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
50
Peptide accession
P14735
Residue number A
789
Residue number B
966
Peptide name
Insulin-degrading enzyme

Ligandability

Cysteine 789 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 966 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.

A redox-regulated disulphide may form within Insulin-degrading enzyme between cysteines 812 and 819. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
3e50
Structure name
crystal structure of human insulin degrading enzyme in complex with transforming growth factor-alpha
Structure deposition date
2008-08-12
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
100
Peptide accession
P14735
Residue number A
812
Residue number B
819
Peptide name
Insulin-degrading enzyme

Ligandability

Cysteine 812 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 819 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.

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