ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

YY1-associated factor 2

Intramolecular
Cysteine 25 and cysteine 39
Cysteine 28 and cysteine 39
Cysteine 39 and cysteine 42
Cysteine 25 and cysteine 28
Cysteine 25 and cysteine 42
Cysteine 28 and cysteine 42
A redox-regulated disulphide may form within YY1-associated factor 2 between cysteines 25 and 39 (14 and 28 respectively in this structure).

Details

Redox score ?
92
PDB code
2d9g
Structure name
solution structure of the zf-ranbp domain of yy1-associated factor 2
Structure deposition date
2005-12-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
0
Peptide accession
Q8IY57
Residue number A
25
Residue number B
39
Peptide name
YY1-associated factor 2

Ligandability

Cysteine 25 of YY1-associated factor 2

Cysteine 39 of YY1-associated factor 2

A redox-regulated disulphide may form within YY1-associated factor 2 between cysteines 28 and 39 (17 and 28 respectively in this structure).

Details

Redox score ?
90
PDB code
2d9g
Structure name
solution structure of the zf-ranbp domain of yy1-associated factor 2
Structure deposition date
2005-12-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
5
% buried
0
Peptide accession
Q8IY57
Residue number A
28
Residue number B
39
Peptide name
YY1-associated factor 2

Ligandability

Cysteine 28 of YY1-associated factor 2

Cysteine 39 of YY1-associated factor 2

A redox-regulated disulphide may form within YY1-associated factor 2 between cysteines 39 and 42 (28 and 31 respectively in this structure).

Details

Redox score ?
90
PDB code
2d9g
Structure name
solution structure of the zf-ranbp domain of yy1-associated factor 2
Structure deposition date
2005-12-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
5
% buried
0
Peptide accession
Q8IY57
Residue number A
39
Residue number B
42
Peptide name
YY1-associated factor 2

Ligandability

Cysteine 39 of YY1-associated factor 2

Cysteine 42 of YY1-associated factor 2

A redox-regulated disulphide may form within YY1-associated factor 2 between cysteines 25 and 28 (14 and 17 respectively in this structure).

Details

Redox score ?
88
PDB code
2d9g
Structure name
solution structure of the zf-ranbp domain of yy1-associated factor 2
Structure deposition date
2005-12-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
7
% buried
0
Peptide accession
Q8IY57
Residue number A
25
Residue number B
28
Peptide name
YY1-associated factor 2

Ligandability

Cysteine 25 of YY1-associated factor 2

Cysteine 28 of YY1-associated factor 2

A redox-regulated disulphide may form within YY1-associated factor 2 between cysteines 25 and 42 (14 and 31 respectively in this structure).

Details

Redox score ?
87
PDB code
2d9g
Structure name
solution structure of the zf-ranbp domain of yy1-associated factor 2
Structure deposition date
2005-12-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
7
% buried
0
Peptide accession
Q8IY57
Residue number A
25
Residue number B
42
Peptide name
YY1-associated factor 2

Ligandability

Cysteine 25 of YY1-associated factor 2

Cysteine 42 of YY1-associated factor 2

A redox-regulated disulphide may form within YY1-associated factor 2 between cysteines 28 and 42 (17 and 31 respectively in this structure).

Details

Redox score ?
79
PDB code
2d9g
Structure name
solution structure of the zf-ranbp domain of yy1-associated factor 2
Structure deposition date
2005-12-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
0
Peptide accession
Q8IY57
Residue number A
28
Residue number B
42
Peptide name
YY1-associated factor 2

Ligandability

Cysteine 28 of YY1-associated factor 2

Cysteine 42 of YY1-associated factor 2

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