ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Fermitin family homolog 3

Intramolecular
Cysteine 623 and cysteine 628
Cysteine 407 and cysteine 452
Cysteine 417 and cysteine 435
Cysteine 439 and cysteine 452
A redox-regulated disulphide may form within Fermitin family homolog 3 between cysteines 623 and 628 (619 and 624 respectively in this structure).

Details

Redox score ?
80
PDB code
6v97
Structure name
kindlin-3 double deletion mutant short form
Structure deposition date
2019-12-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
67
Peptide accession
Q86UX7
Residue number A
623
Residue number B
628
Peptide name
Fermitin family homolog 3

Ligandability

Cysteine 623 of Fermitin family homolog 3

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 628 of Fermitin family homolog 3

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 3 between cysteines 407 and 452. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7c3m
Structure name
structure of ferm protein
Structure deposition date
2020-05-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
68
Peptide accession
Q86UX7
Residue number A
407
Residue number B
452
Peptide name
Fermitin family homolog 3

Ligandability

Cysteine 407 of Fermitin family homolog 3

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 452 of Fermitin family homolog 3

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 3 between cysteines 417 and 435. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5l81
Structure name
crystal structure of the ph domain of murine kindlin-3
Structure deposition date
2016-06-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
67
Minimum pKa ?
11
% buried
90
Peptide accession
Q8K1B8
Residue number A
417
Residue number B
435
Peptide name
Fermitin family homolog 3

Ligandability

Cysteine 417 of Fermitin family homolog 3

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 435 of Fermitin family homolog 3

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 3 between cysteines 439 and 452. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
7c3m
Structure name
structure of ferm protein
Structure deposition date
2020-05-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
12
% buried
94
Peptide accession
Q86UX7
Residue number A
439
Residue number B
452
Peptide name
Fermitin family homolog 3

Ligandability

Cysteine 439 of Fermitin family homolog 3

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 452 of Fermitin family homolog 3

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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