ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger CCCH-type with G patch domain-containing protein

Intramolecular
Cysteine 180 and cysteine 188
Cysteine 180 and cysteine 194
Cysteine 188 and cysteine 194
A redox-regulated disulphide may form within Zinc finger CCCH-type with G patch domain-containing protein between cysteines 180 and 188.

Details

Redox score ?
80
PDB code
4ii1
Structure name
crystal structure of the zinc finger of zgpat
Structure deposition date
2012-12-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N5A5
Residue number A
180
Residue number B
188
Peptide name
Zinc finger CCCH-type with G patch domain-containing protein

Ligandability

Cysteine 180 of Zinc finger CCCH-type with G patch domain-containing protein

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 188 of Zinc finger CCCH-type with G patch domain-containing protein

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 CCCH-type with G patch domain-containing protein between cysteines 180 and 194.

Details

Redox score ?
79
PDB code
4ii1
Structure name
crystal structure of the zinc finger of zgpat
Structure deposition date
2012-12-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N5A5
Residue number A
180
Residue number B
194
Peptide name
Zinc finger CCCH-type with G patch domain-containing protein

Ligandability

Cysteine 180 of Zinc finger CCCH-type with G patch domain-containing protein

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 194 of Zinc finger CCCH-type with G patch domain-containing protein

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 CCCH-type with G patch domain-containing protein between cysteines 188 and 194.

Details

Redox score ?
78
PDB code
4ii1
Structure name
crystal structure of the zinc finger of zgpat
Structure deposition date
2012-12-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8N5A5
Residue number A
188
Residue number B
194
Peptide name
Zinc finger CCCH-type with G patch domain-containing protein

Ligandability

Cysteine 188 of Zinc finger CCCH-type with G patch domain-containing protein

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 194 of Zinc finger CCCH-type with G patch domain-containing protein

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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