ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Erythroid transcription factor

Intramolecular
Cysteine 261 and cysteine 282
Cysteine 258 and cysteine 282
Cysteine 204 and cysteine 207
Cysteine 279 and cysteine 282
Cysteine 204 and cysteine 228
Cysteine 204 and cysteine 225
Cysteine 258 and cysteine 261
Cysteine 207 and cysteine 228
Cysteine 207 and cysteine 225
Cysteine 258 and cysteine 279
More...
Cysteine 225 and cysteine 228
Cysteine 261 and cysteine 279
A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 261 and 282.

Details

Redox score ?
91
PDB code
3vek
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p1 crystal form
Structure deposition date
2012-01-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
60
Minimum pKa ?
3
% buried
46
Peptide accession
P17679
Residue number A
261
Residue number B
282
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 261 of Erythroid transcription factor

Cysteine 282 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 258 and 282.

Details

Redox score ?
90
PDB code
3vek
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p1 crystal form
Structure deposition date
2012-01-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
3
% buried
48
Peptide accession
P17679
Residue number A
258
Residue number B
282
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 258 of Erythroid transcription factor

Cysteine 282 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 204 and 207.

Details

Redox score ?
88
PDB code
3vd6
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p21 crystal form
Structure deposition date
2012-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
18
Peptide accession
P17679
Residue number A
204
Residue number B
207
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 204 of Erythroid transcription factor

Cysteine 207 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 279 and 282.

Details

Redox score ?
87
PDB code
3vek
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p1 crystal form
Structure deposition date
2012-01-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
65
Minimum pKa ?
3
% buried
64
Peptide accession
P17679
Residue number A
279
Residue number B
282
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 279 of Erythroid transcription factor

Cysteine 282 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 204 and 228.

Details

Redox score ?
86
PDB code
3vd6
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p21 crystal form
Structure deposition date
2012-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
60
Minimum pKa ?
5
% buried
28
Peptide accession
P17679
Residue number A
204
Residue number B
228
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 204 of Erythroid transcription factor

Cysteine 228 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 204 and 225.

Details

Redox score ?
85
PDB code
3vd6
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p21 crystal form
Structure deposition date
2012-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
34
Peptide accession
P17679
Residue number A
204
Residue number B
225
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 204 of Erythroid transcription factor

Cysteine 225 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 258 and 261.

Details

Redox score ?
83
PDB code
3vd6
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p21 crystal form
Structure deposition date
2012-01-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
7
% buried
36
Peptide accession
P17679
Residue number A
258
Residue number B
261
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 258 of Erythroid transcription factor

Cysteine 261 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 207 and 228.

Details

Redox score ?
80
PDB code
3vek
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p1 crystal form
Structure deposition date
2012-01-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
21
Peptide accession
P17679
Residue number A
207
Residue number B
228
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 207 of Erythroid transcription factor

Cysteine 228 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 207 and 225.

Details

Redox score ?
79
PDB code
3vek
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p1 crystal form
Structure deposition date
2012-01-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
25
Peptide accession
P17679
Residue number A
207
Residue number B
225
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 207 of Erythroid transcription factor

Cysteine 225 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 258 and 279.

Details

Redox score ?
76
PDB code
3vek
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p1 crystal form
Structure deposition date
2012-01-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
8
% buried
56
Peptide accession
P17679
Residue number A
258
Residue number B
279
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 258 of Erythroid transcription factor

Cysteine 279 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 225 and 228.

Details

Redox score ?
76
PDB code
3vek
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p1 crystal form
Structure deposition date
2012-01-09
Thiol separation (Å)
3
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
36
Peptide accession
P17679
Residue number A
225
Residue number B
228
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 225 of Erythroid transcription factor

Cysteine 228 of Erythroid transcription factor

A redox-regulated disulphide may form within Erythroid transcription factor between cysteines 261 and 279.

Details

Redox score ?
71
PDB code
3vek
Structure name
both zn fingers of gata1 bound to palindromic dna recognition site, p1 crystal form
Structure deposition date
2012-01-09
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
10
% buried
54
Peptide accession
P17679
Residue number A
261
Residue number B
279
Peptide name
Erythroid transcription factor

Ligandability

Cysteine 261 of Erythroid transcription factor

Cysteine 279 of Erythroid transcription factor

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