ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Fermitin family homolog 2

Intramolecular
Cysteine 397 and cysteine 406
Cysteine 638 and cysteine 643
Cysteine 426 and cysteine 471
Cysteine 397 and cysteine 471
Cysteine 458 and cysteine 471
Cysteine 397 and cysteine 426
Cysteine 397 and cysteine 458
A redox-regulated disulphide may form within Fermitin family homolog 2 between cysteines 397 and 406.

Details

Redox score ?
71
PDB code
4f7h
Structure name
the crystal structure of kindlin-2 pleckstrin homology domain in free form
Structure deposition date
2012-05-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
73
Minimum pKa ?
8
% buried
80
Peptide accession
Q96AC1
Residue number A
397
Residue number B
406
Peptide name
Fermitin family homolog 2

Ligandability

Cysteine 397 of Fermitin family homolog 2

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 406 of Fermitin family homolog 2

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 Fermitin family homolog 2 between cysteines 638 and 643.

Details

Redox score ?
66
PDB code
5xpz
Structure name
structural basis of kindlin-mediated integrin recognition and activation
Structure deposition date
2017-06-05
Thiol separation (Å)
5
Half-sphere exposure sum ?
65
Minimum pKa ?
10
% buried
56
Peptide accession
Q8CIB5
Residue number A
638
Residue number B
643
Peptide name
Fermitin family homolog 2

Ligandability

Cysteine 638 of Fermitin family homolog 2

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 643 of Fermitin family homolog 2

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 Fermitin family homolog 2 between cysteines 426 and 471. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4f7h
Structure name
the crystal structure of kindlin-2 pleckstrin homology domain in free form
Structure deposition date
2012-05-16
Thiol separation (Å)
6
Half-sphere exposure sum ?
77
Minimum pKa ?
11
% buried
78
Peptide accession
Q96AC1
Residue number A
426
Residue number B
471
Peptide name
Fermitin family homolog 2

Ligandability

Cysteine 426 of Fermitin family homolog 2

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 471 of Fermitin family homolog 2

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 Fermitin family homolog 2 between cysteines 397 and 471. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
2lko
Structure name
structural basis of phosphoinositide binding to kindlin-2 pleckstrin homology domain in regulating integrin activation
Structure deposition date
2011-10-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
86
Peptide accession
Q96AC1
Residue number A
397
Residue number B
471
Peptide name
Fermitin family homolog 2

Ligandability

Cysteine 397 of Fermitin family homolog 2

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 471 of Fermitin family homolog 2

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 Fermitin family homolog 2 between cysteines 458 and 471. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4f7h
Structure name
the crystal structure of kindlin-2 pleckstrin homology domain in free form
Structure deposition date
2012-05-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
94
Peptide accession
Q96AC1
Residue number A
458
Residue number B
471
Peptide name
Fermitin family homolog 2

Ligandability

Cysteine 458 of Fermitin family homolog 2

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 471 of Fermitin family homolog 2

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 Fermitin family homolog 2 between cysteines 397 and 426. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
2lko
Structure name
structural basis of phosphoinositide binding to kindlin-2 pleckstrin homology domain in regulating integrin activation
Structure deposition date
2011-10-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
66
Minimum pKa ?
10
% buried
72
Peptide accession
Q96AC1
Residue number A
397
Residue number B
426
Peptide name
Fermitin family homolog 2

Ligandability

Cysteine 397 of Fermitin family homolog 2

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 426 of Fermitin family homolog 2

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 Fermitin family homolog 2 between cysteines 397 and 458. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4f7h
Structure name
the crystal structure of kindlin-2 pleckstrin homology domain in free form
Structure deposition date
2012-05-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
86
Peptide accession
Q96AC1
Residue number A
397
Residue number B
458
Peptide name
Fermitin family homolog 2

Ligandability

Cysteine 397 of Fermitin family homolog 2

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 458 of Fermitin family homolog 2

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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