ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Interleukin enhancer-binding factor 3

Intermolecular
Cysteine 37 of Interleukin enhancer-binding factor 2 and cysteine 278
Intramolecular
Cysteine 226 and cysteine 255
Cysteine 116 and cysteine 203 L
Cysteine 237 and cysteine 255
Cysteine 255 and cysteine 278
A redox-regulated disulphide may form between cysteine 37 of Interleukin enhancer-binding factor 2 and cysteine 278 of Interleukin enhancer-binding factor 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4at7
Structure name
crystal structure of the nf90-nf45 dimerisation domain complex
Structure deposition date
2012-05-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
75
Minimum pKa ?
11
% buried
87
Peptide A name
Interleukin enhancer-binding factor 2
Peptide B name
Interleukin enhancer-binding factor 3
Peptide A accession
Q9CXY6
Peptide B accession
Q9Z1X4
Peptide A residue number
37
Peptide B residue number
278

Ligandability

Cysteine 37 of Interleukin enhancer-binding factor 2

Cysteine 278 of Interleukin enhancer-binding factor 3

A redox-regulated disulphide may form within Interleukin enhancer-binding factor 3 between cysteines 226 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
4atb
Structure name
crystal structure of the nf90-nf45 dimerisation domain complex with ctp
Structure deposition date
2012-05-05
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
13
% buried
100
Peptide accession
Q9Z1X4
Residue number A
226
Residue number B
255
Peptide name
Interleukin enhancer-binding factor 3

Ligandability

Cysteine 226 of Interleukin enhancer-binding factor 3

Cysteine 255 of Interleukin enhancer-binding factor 3

A redox-regulated disulphide may form within Interleukin enhancer-binding factor 3 between cysteines 116 and 203. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4atb
Structure name
crystal structure of the nf90-nf45 dimerisation domain complex with ctp
Structure deposition date
2012-05-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
11
% buried
67
Peptide accession
Q9Z1X4
Residue number A
116
Residue number B
203
Peptide name
Interleukin enhancer-binding factor 3

Ligandability

Cysteine 116 of Interleukin enhancer-binding factor 3

Cysteine 203 of Interleukin enhancer-binding factor 3

A redox-regulated disulphide may form within Interleukin enhancer-binding factor 3 between cysteines 237 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
4atb
Structure name
crystal structure of the nf90-nf45 dimerisation domain complex with ctp
Structure deposition date
2012-05-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
90
Peptide accession
Q9Z1X4
Residue number A
237
Residue number B
255
Peptide name
Interleukin enhancer-binding factor 3

Ligandability

Cysteine 237 of Interleukin enhancer-binding factor 3

Cysteine 255 of Interleukin enhancer-binding factor 3

A redox-regulated disulphide may form within Interleukin enhancer-binding factor 3 between cysteines 255 and 278. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
4atb
Structure name
crystal structure of the nf90-nf45 dimerisation domain complex with ctp
Structure deposition date
2012-05-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide accession
Q9Z1X4
Residue number A
255
Residue number B
278
Peptide name
Interleukin enhancer-binding factor 3

Ligandability

Cysteine 255 of Interleukin enhancer-binding factor 3

Cysteine 278 of Interleukin enhancer-binding factor 3

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