ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Influenza virus NS1A-binding protein

Intramolecular
Cysteine 482 and cysteine 495 L
Cysteine 459 and cysteine 508
Cysteine 52 and cysteine 53
Cysteine 381 and cysteine 454
A redox-regulated disulphide may form within Influenza virus NS1A-binding protein between cysteines 482 and 495.

Details

Redox score ?
76
PDB code
6n3h
Structure name
crystal structure of kelch domain of the human ns1 binding protein
Structure deposition date
2018-11-15
Thiol separation (Å)
5
Half-sphere exposure sum ?
62
Minimum pKa ?
7
% buried
67
Peptide accession
Q9Y6Y0
Residue number A
482
Residue number B
495
Peptide name
Influenza virus NS1A-binding protein

Ligandability

Cysteine 482 of Influenza virus NS1A-binding 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 495 of Influenza virus NS1A-binding 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Influenza virus NS1A-binding protein between cysteines 459 and 508. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
6n3h
Structure name
crystal structure of kelch domain of the human ns1 binding protein
Structure deposition date
2018-11-15
Thiol separation (Å)
7
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
Q9Y6Y0
Residue number A
459
Residue number B
508
Peptide name
Influenza virus NS1A-binding protein

Ligandability

Cysteine 459 of Influenza virus NS1A-binding 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 508 of Influenza virus NS1A-binding 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 Influenza virus NS1A-binding protein between cysteines 52 and 53. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6n34
Structure name
crystal structure of the btb domain of human ns1-bp
Structure deposition date
2018-11-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
95
Peptide accession
Q9Y6Y0
Residue number A
52
Residue number B
53
Peptide name
Influenza virus NS1A-binding protein

Ligandability

Cysteine 52 of Influenza virus NS1A-binding 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 53 of Influenza virus NS1A-binding 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 Influenza virus NS1A-binding protein between cysteines 381 and 454. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
6n3h
Structure name
crystal structure of kelch domain of the human ns1 binding protein
Structure deposition date
2018-11-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
57
Peptide accession
Q9Y6Y0
Residue number A
381
Residue number B
454
Peptide name
Influenza virus NS1A-binding protein

Ligandability

Cysteine 381 of Influenza virus NS1A-binding 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 454 of Influenza virus NS1A-binding 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.

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