ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Zinc finger MYM-type protein 5

Intramolecular
Cysteine 244 and cysteine 272
Cysteine 244 and cysteine 247
Cysteine 244 and cysteine 268
Cysteine 268 and cysteine 272
Cysteine 247 and cysteine 272
Cysteine 247 and cysteine 268
A redox-regulated disulphide may form within Zinc finger MYM-type protein 5 between cysteines 244 and 272 (23 and 51 respectively in this structure).

Details

Redox score ?
90
PDB code
2das
Structure name
solution structure of trash domain of zinc finger mym-type protein 5
Structure deposition date
2005-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
0
Peptide accession
Q9UJ78
Residue number A
244
Residue number B
272
Peptide name
Zinc finger MYM-type protein 5

Ligandability

Cysteine 244 of Zinc finger MYM-type protein 5

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 272 of Zinc finger MYM-type protein 5

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 MYM-type protein 5 between cysteines 244 and 247 (23 and 26 respectively in this structure).

Details

Redox score ?
89
PDB code
2das
Structure name
solution structure of trash domain of zinc finger mym-type protein 5
Structure deposition date
2005-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
0
Peptide accession
Q9UJ78
Residue number A
244
Residue number B
247
Peptide name
Zinc finger MYM-type protein 5

Ligandability

Cysteine 244 of Zinc finger MYM-type protein 5

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 247 of Zinc finger MYM-type protein 5

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 MYM-type protein 5 between cysteines 244 and 268 (23 and 47 respectively in this structure).

Details

Redox score ?
87
PDB code
2das
Structure name
solution structure of trash domain of zinc finger mym-type protein 5
Structure deposition date
2005-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
0
Peptide accession
Q9UJ78
Residue number A
244
Residue number B
268
Peptide name
Zinc finger MYM-type protein 5

Ligandability

Cysteine 244 of Zinc finger MYM-type protein 5

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 268 of Zinc finger MYM-type protein 5

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 MYM-type protein 5 between cysteines 268 and 272 (47 and 51 respectively in this structure).

Details

Redox score ?
80
PDB code
2das
Structure name
solution structure of trash domain of zinc finger mym-type protein 5
Structure deposition date
2005-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
9
% buried
0
Peptide accession
Q9UJ78
Residue number A
268
Residue number B
272
Peptide name
Zinc finger MYM-type protein 5

Ligandability

Cysteine 268 of Zinc finger MYM-type protein 5

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 272 of Zinc finger MYM-type protein 5

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 MYM-type protein 5 between cysteines 247 and 272 (26 and 51 respectively in this structure).

Details

Redox score ?
77
PDB code
2das
Structure name
solution structure of trash domain of zinc finger mym-type protein 5
Structure deposition date
2005-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
Q9UJ78
Residue number A
247
Residue number B
272
Peptide name
Zinc finger MYM-type protein 5

Ligandability

Cysteine 247 of Zinc finger MYM-type protein 5

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 272 of Zinc finger MYM-type protein 5

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 MYM-type protein 5 between cysteines 247 and 268 (26 and 47 respectively in this structure).

Details

Redox score ?
77
PDB code
2das
Structure name
solution structure of trash domain of zinc finger mym-type protein 5
Structure deposition date
2005-12-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
9
% buried
0
Peptide accession
Q9UJ78
Residue number A
247
Residue number B
268
Peptide name
Zinc finger MYM-type protein 5

Ligandability

Cysteine 247 of Zinc finger MYM-type protein 5

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 268 of Zinc finger MYM-type protein 5

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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