ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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FAS-associated factor 1

Intramolecular
Cysteine 348 and cysteine 396
Cysteine 348 and cysteine 391
Cysteine 391 and cysteine 396
A redox-regulated disulphide may form within FAS-associated factor 1 between cysteines 348 and 396 (31 and 79 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2ec4
Structure name
solution structure of the uas domain from human fas-associated factor 1
Structure deposition date
2007-02-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
5
Peptide accession
Q9UNN5
Residue number A
348
Residue number B
396
Peptide name
FAS-associated factor 1

Ligandability

Cysteine 348 of FAS-associated factor 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 396 of FAS-associated factor 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 FAS-associated factor 1 between cysteines 348 and 391 (31 and 74 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2ec4
Structure name
solution structure of the uas domain from human fas-associated factor 1
Structure deposition date
2007-02-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
30
Peptide accession
Q9UNN5
Residue number A
348
Residue number B
391
Peptide name
FAS-associated factor 1

Ligandability

Cysteine 348 of FAS-associated factor 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 391 of FAS-associated factor 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 FAS-associated factor 1 between cysteines 391 and 396 (74 and 79 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
2ec4
Structure name
solution structure of the uas domain from human fas-associated factor 1
Structure deposition date
2007-02-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
35
Peptide accession
Q9UNN5
Residue number A
391
Residue number B
396
Peptide name
FAS-associated factor 1

Ligandability

Cysteine 391 of FAS-associated factor 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 396 of FAS-associated factor 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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