a tool for identifying drug-targetable redox-active disulphides

IGL@ protein

Intramolecular

Cysteine 156 and cysteine 215

Cysteine 41 and cysteine 106

Cysteine 14 and cysteine 106

Cysteine 41 and cysteine 14

A redox-regulated disulphide may form within IGL@ protein between cysteines 156 and 215 (136 and 195 respectively in this structure).

Details

Redox score ?

79

PDB code

Structure name

influenza hemagglutinin in complex with a neutralizing antibody

Structure deposition date

2017-01-10

Thiol separation (Å)

2

Half-sphere exposure sum ?

87

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

156

Residue number B

215

Peptide name

IGL@ protein

Ligandability

Cysteine 156 of IGL@ protein

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 215 of IGL@ protein

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 IGL@ protein between cysteines 41 and 106 (23 and 88 respectively in this structure).

Details

Redox score ?

79

PDB code

Structure name

i33m (i3

Structure deposition date

2020-02-04

Thiol separation (Å)

2

Half-sphere exposure sum ?

92

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Residue number A

41

Residue number B

106

Peptide name

IGL@ protein

Ligandability

Cysteine 41 of IGL@ protein

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 106 of IGL@ protein

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 IGL@ protein between cysteines 14 and 106 (34 and 88 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

36

PDB code

Structure name

i33m (i3

Structure deposition date

2020-02-04

Thiol separation (Å)

8

Half-sphere exposure sum ?

94

Minimum pK_a ?

12

% buried

nan

Peptide accession

Residue number A

14

Residue number B

106

Peptide name

IGL@ protein

Ligandability

Cysteine 14 of IGL@ protein

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 106 of IGL@ protein

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.

Uncertain whether structure cysteine 34 has been assigned to correct residue.

A redox-regulated disulphide may form within IGL@ protein between cysteines 41 and 14 (23 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 ?

31

PDB code

Structure name

i33m (i3

Structure deposition date

2020-02-04

Thiol separation (Å)

9

Half-sphere exposure sum ?

86

Minimum pK_a ?

12

% buried

nan

Peptide accession

Residue number A

41

Residue number B

14

Peptide name

IGL@ protein

Ligandability

Cysteine 41 of IGL@ protein

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 14 of IGL@ protein

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.

Uncertain whether structure cysteine 34 has been assigned to correct residue.

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