ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Fanconi anemia group E protein

Intramolecular
Cysteine 319 and cysteine 328
Cysteine 421 and cysteine 422
Cysteine 399 and cysteine 422
A redox-regulated disulphide may form within Fanconi anemia group E protein between cysteines 319 and 328. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
2ilr
Structure name
crystal structure of human fanconi anemia protein e c-terminal domain
Structure deposition date
2006-10-03
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
11
% buried
68
Peptide accession
Q9HB96
Residue number A
319
Residue number B
328
Peptide name
Fanconi anemia group E protein

Ligandability

Cysteine 319 of Fanconi anemia group E protein

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 328 of Fanconi anemia group E protein

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 Fanconi anemia group E protein between cysteines 421 and 422. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
2ilr
Structure name
crystal structure of human fanconi anemia protein e c-terminal domain
Structure deposition date
2006-10-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
50
Peptide accession
Q9HB96
Residue number A
421
Residue number B
422
Peptide name
Fanconi anemia group E protein

Ligandability

Cysteine 421 of Fanconi anemia group E protein

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 422 of Fanconi anemia group E protein

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 Fanconi anemia group E protein between cysteines 399 and 422. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
2ilr
Structure name
crystal structure of human fanconi anemia protein e c-terminal domain
Structure deposition date
2006-10-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
64
Peptide accession
Q9HB96
Residue number A
399
Residue number B
422
Peptide name
Fanconi anemia group E protein

Ligandability

Cysteine 399 of Fanconi anemia group E protein

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 422 of Fanconi anemia group E protein

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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