ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Nck-associated protein 1

Intermolecular
Cysteine 731 of Cytoplasmic FMR1-interacting protein 1 and cysteine 633
Intramolecular
Cysteine 573 and cysteine 599
Cysteine 543 and cysteine 579
Cysteine 618 and cysteine 622
Cysteine 543 and cysteine 573
Cysteine 579 and cysteine 584
A redox-regulated disulphide may form between cysteine 731 of Cytoplasmic FMR1-interacting protein 1 and cysteine 633 of Nck-associated protein 1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4n78
Structure name
the wave regulatory complex links diverse receptors to the actin cytoskeleton
Structure deposition date
2013-10-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
54
Peptide A name
Cytoplasmic FMR1-interacting protein 1
Peptide B name
Nck-associated protein 1
Peptide A accession
Q7L576
Peptide B accession
Q9Y2A7
Peptide A residue number
731
Peptide B residue number
633

Ligandability

Cysteine 731 of Cytoplasmic FMR1-interacting protein 1

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 633 of Nck-associated protein 1

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 Nck-associated protein 1 between cysteines 573 and 599.

Details

Redox score ?
61
PDB code
3p8c
Structure name
structure and control of the actin regulatory wave complex
Structure deposition date
2010-10-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
85
Minimum pKa ?
9
% buried
100
Peptide accession
Q9Y2A7
Residue number A
573
Residue number B
599
Peptide name
Nck-associated protein 1

Ligandability

Cysteine 573 of Nck-associated protein 1

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 599 of Nck-associated protein 1

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 Nck-associated protein 1 between cysteines 543 and 579. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3p8c
Structure name
structure and control of the actin regulatory wave complex
Structure deposition date
2010-10-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
76
Peptide accession
Q9Y2A7
Residue number A
543
Residue number B
579
Peptide name
Nck-associated protein 1

Ligandability

Cysteine 543 of Nck-associated protein 1

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 579 of Nck-associated protein 1

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 Nck-associated protein 1 between cysteines 618 and 622. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
3p8c
Structure name
structure and control of the actin regulatory wave complex
Structure deposition date
2010-10-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
85
Peptide accession
Q9Y2A7
Residue number A
618
Residue number B
622
Peptide name
Nck-associated protein 1

Ligandability

Cysteine 618 of Nck-associated protein 1

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 622 of Nck-associated protein 1

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 Nck-associated protein 1 between cysteines 543 and 573. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
4n78
Structure name
the wave regulatory complex links diverse receptors to the actin cytoskeleton
Structure deposition date
2013-10-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
11
% buried
86
Peptide accession
Q9Y2A7
Residue number A
543
Residue number B
573
Peptide name
Nck-associated protein 1

Ligandability

Cysteine 543 of Nck-associated protein 1

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 573 of Nck-associated protein 1

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 Nck-associated protein 1 between cysteines 579 and 584. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4n78
Structure name
the wave regulatory complex links diverse receptors to the actin cytoskeleton
Structure deposition date
2013-10-15
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
80
Peptide accession
Q9Y2A7
Residue number A
579
Residue number B
584
Peptide name
Nck-associated protein 1

Ligandability

Cysteine 579 of Nck-associated protein 1

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 584 of Nck-associated protein 1

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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