ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger protein Eos

Intramolecular
Cysteine 189 and cysteine 192
Cysteine 161 and cysteine 164
Cysteine 164 and cysteine 168
A redox-regulated disulphide may form within Zinc finger protein Eos between cysteines 189 and 192 (46 and 49 respectively in this structure).

Details

Redox score ?
80
PDB code
2ma7
Structure name
solution nmr structure of zinc finger protein eos from homo sapiens, northeast structural genomics consortium (nesg) target hr7992a
Structure deposition date
2013-06-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
35
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9H2S9
Residue number A
189
Residue number B
192
Peptide name
Zinc finger protein Eos

Ligandability

Cysteine 189 of Zinc finger protein Eos

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 192 of Zinc finger protein Eos

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 Zinc finger protein Eos between cysteines 161 and 164 (18 and 21 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
2ma7
Structure name
solution nmr structure of zinc finger protein eos from homo sapiens, northeast structural genomics consortium (nesg) target hr7992a
Structure deposition date
2013-06-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
13
Minimum pKa ?
9
% buried
0
Peptide accession
Q9H2S9
Residue number A
161
Residue number B
164
Peptide name
Zinc finger protein Eos

Ligandability

Cysteine 161 of Zinc finger protein Eos

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 164 of Zinc finger protein Eos

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 Zinc finger protein Eos between cysteines 164 and 168 (21 and 25 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
2ma7
Structure name
solution nmr structure of zinc finger protein eos from homo sapiens, northeast structural genomics consortium (nesg) target hr7992a
Structure deposition date
2013-06-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
13
Minimum pKa ?
9
% buried
0
Peptide accession
Q9H2S9
Residue number A
164
Residue number B
168
Peptide name
Zinc finger protein Eos

Ligandability

Cysteine 164 of Zinc finger protein Eos

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 168 of Zinc finger protein Eos

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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