ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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FERM, ARHGEF and pleckstrin domain-containing protein 2

Intramolecular
Cysteine 699 and cysteine 712
Cysteine 764 and cysteine 913
Cysteine 306 and cysteine 313
A redox-regulated disulphide may form within FERM, ARHGEF and pleckstrin domain-containing protein 2 between cysteines 699 and 712.

Details

Redox score ?
68
PDB code
4gzu
Structure name
crystal structure of the dh-ph-ph domain of farp2
Structure deposition date
2012-09-06
Thiol separation (Å)
5
Half-sphere exposure sum ?
57
Minimum pKa ?
10
% buried
24
Peptide accession
Q91VS8
Residue number A
699
Residue number B
712
Peptide name
FERM, ARHGEF and pleckstrin domain-containing protein 2

Ligandability

Cysteine 699 of FERM, ARHGEF and pleckstrin domain-containing protein 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 712 of FERM, ARHGEF and pleckstrin domain-containing protein 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 FERM, ARHGEF and pleckstrin domain-containing protein 2 between cysteines 764 and 913. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4gzu
Structure name
crystal structure of the dh-ph-ph domain of farp2
Structure deposition date
2012-09-06
Thiol separation (Å)
8
Half-sphere exposure sum ?
71
Minimum pKa ?
12
% buried
88
Peptide accession
Q91VS8
Residue number A
764
Residue number B
913
Peptide name
FERM, ARHGEF and pleckstrin domain-containing protein 2

Ligandability

Cysteine 764 of FERM, ARHGEF and pleckstrin domain-containing protein 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 913 of FERM, ARHGEF and pleckstrin domain-containing protein 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 FERM, ARHGEF and pleckstrin domain-containing protein 2 between cysteines 306 and 313. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
6d2k
Structure name
crystal structure of the ferm domain of mouse farp2
Structure deposition date
2018-04-13
Thiol separation (Å)
10
Half-sphere exposure sum ?
70
Minimum pKa ?
11
% buried
72
Peptide accession
Q91VS8
Residue number A
306
Residue number B
313
Peptide name
FERM, ARHGEF and pleckstrin domain-containing protein 2

Ligandability

Cysteine 306 of FERM, ARHGEF and pleckstrin domain-containing protein 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 313 of FERM, ARHGEF and pleckstrin domain-containing protein 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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