ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Cytoplasmic FMR1-interacting protein 1

Intermolecular
Cysteine 731 and cysteine 633 of Nck-associated protein 1
Intramolecular
Cysteine 1087 and cysteine 1088
Cysteine 1139 and cysteine 1180
Cysteine 960 and cysteine 1124
Cysteine 615 and cysteine 616
Cysteine 856 and cysteine 1152
Cysteine 1020 and cysteine 1087
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 Cytoplasmic FMR1-interacting protein 1 between cysteines 1087 and 1088.

Details

Redox score ?
74
PDB code
3p8c
Structure name
structure and control of the actin regulatory wave complex
Structure deposition date
2010-10-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
6
% buried
72
Peptide accession
Q7L576
Residue number A
1087
Residue number B
1088
Peptide name
Cytoplasmic FMR1-interacting protein 1

Ligandability

Cysteine 1087 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 1088 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.

A redox-regulated disulphide may form within Cytoplasmic FMR1-interacting protein 1 between cysteines 1139 and 1180.

Details

Redox score ?
68
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)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
10
% buried
100
Peptide accession
Q7L576
Residue number A
1139
Residue number B
1180
Peptide name
Cytoplasmic FMR1-interacting protein 1

Ligandability

Cysteine 1139 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 1180 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.

A redox-regulated disulphide may form within Cytoplasmic FMR1-interacting protein 1 between cysteines 960 and 1124.

Details

Redox score ?
64
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)
5
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
80
Peptide accession
Q7L576
Residue number A
960
Residue number B
1124
Peptide name
Cytoplasmic FMR1-interacting protein 1

Ligandability

Cysteine 960 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 1124 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.

A redox-regulated disulphide may form within Cytoplasmic FMR1-interacting protein 1 between cysteines 615 and 616. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
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 ?
82
Minimum pKa ?
13
% buried
96
Peptide accession
Q7L576
Residue number A
615
Residue number B
616
Peptide name
Cytoplasmic FMR1-interacting protein 1

Ligandability

Cysteine 615 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 616 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.

A redox-regulated disulphide may form within Cytoplasmic FMR1-interacting protein 1 between cysteines 856 and 1152. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
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 ?
84
Minimum pKa ?
11
% buried
88
Peptide accession
Q7L576
Residue number A
856
Residue number B
1152
Peptide name
Cytoplasmic FMR1-interacting protein 1

Ligandability

Cysteine 856 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 1152 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.

A redox-regulated disulphide may form within Cytoplasmic FMR1-interacting protein 1 between cysteines 1020 and 1087. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
3p8c
Structure name
structure and control of the actin regulatory wave complex
Structure deposition date
2010-10-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
94
Peptide accession
Q7L576
Residue number A
1020
Residue number B
1087
Peptide name
Cytoplasmic FMR1-interacting protein 1

Ligandability

Cysteine 1020 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 1087 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.

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