ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

CCAAT/enhancer-binding protein epsilon

Intramolecular
Cysteine 280 and cysteine 60
Cysteine 148 and cysteine 84
Cysteine 148 and cysteine 79
Cysteine 49 and cysteine 280
Cysteine 49 and cysteine 60
A redox-regulated disulphide may form within CCAAT/enhancer-binding protein epsilon between cysteines 280 and 60 (57 and 60 respectively in this structure).

Details

Redox score ?
nan
PDB code
3t92
Structure name
crystal structure of the taz2:c/ebpepsilon-tad chimera protein
Structure deposition date
2011-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
0
Peptide accession
Q15744
Residue number A
280
Residue number B
60
Peptide name
CCAAT/enhancer-binding protein epsilon

Ligandability

Cysteine 280 of CCAAT/enhancer-binding protein epsilon

Cysteine 60 of CCAAT/enhancer-binding protein epsilon

Uncertain whether structure cysteine 57 has been assigned to correct residue.
Cysteine 60 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within CCAAT/enhancer-binding protein epsilon between cysteines 148 and 84 (74 and 84 respectively in this structure).

Details

Redox score ?
nan
PDB code
3t92
Structure name
crystal structure of the taz2:c/ebpepsilon-tad chimera protein
Structure deposition date
2011-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
15
Peptide accession
Q15744
Residue number A
148
Residue number B
84
Peptide name
CCAAT/enhancer-binding protein epsilon

Ligandability

Cysteine 148 of CCAAT/enhancer-binding protein epsilon

Cysteine 84 of CCAAT/enhancer-binding protein epsilon

Uncertain whether structure cysteine 74 has been assigned to correct residue.
Cysteine 84 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within CCAAT/enhancer-binding protein epsilon between cysteines 148 and 79 (74 and 79 respectively in this structure).

Details

Redox score ?
nan
PDB code
3t92
Structure name
crystal structure of the taz2:c/ebpepsilon-tad chimera protein
Structure deposition date
2011-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
7
% buried
15
Peptide accession
Q15744
Residue number A
148
Residue number B
79
Peptide name
CCAAT/enhancer-binding protein epsilon

Ligandability

Cysteine 148 of CCAAT/enhancer-binding protein epsilon

Cysteine 79 of CCAAT/enhancer-binding protein epsilon

Uncertain whether structure cysteine 74 has been assigned to correct residue.
Cysteine 79 in protein B could not be asigned to a Uniprot residue.
A redox-regulated disulphide may form within CCAAT/enhancer-binding protein epsilon between cysteines 49 and 280 (49 and 57 respectively in this structure).

Details

Redox score ?
nan
PDB code
3t92
Structure name
crystal structure of the taz2:c/ebpepsilon-tad chimera protein
Structure deposition date
2011-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
6
% buried
0
Peptide accession
Q15744
Residue number A
49
Residue number B
280
Peptide name
CCAAT/enhancer-binding protein epsilon

Ligandability

Cysteine 49 of CCAAT/enhancer-binding protein epsilon

Cysteine 280 of CCAAT/enhancer-binding protein epsilon

Cysteine 49 in protein A could not be asigned to a Uniprot residue.
Uncertain whether structure cysteine 57 has been assigned to correct residue.
A redox-regulated disulphide may form within CCAAT/enhancer-binding protein epsilon between cysteines 49 and 60.

Details

Redox score ?
nan
PDB code
3t92
Structure name
crystal structure of the taz2:c/ebpepsilon-tad chimera protein
Structure deposition date
2011-08-02
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
0
Peptide accession
Q15744
Residue number A
49
Residue number B
60
Peptide name
CCAAT/enhancer-binding protein epsilon

Ligandability

Cysteine 49 of CCAAT/enhancer-binding protein epsilon

Cysteine 60 of CCAAT/enhancer-binding protein epsilon

Cysteine 49 in protein A could not be asigned to a Uniprot residue.
Cysteine 60 in protein B could not be asigned to a Uniprot residue.
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