ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Dachshund homolog 1

Intramolecular
Cysteine 243 and cysteine 264
Cysteine 210 and cysteine 264
Cysteine 188 and cysteine 243
Cysteine 210 and cysteine 243
Cysteine 188 and cysteine 210
A redox-regulated disulphide may form within Dachshund homolog 1 between cysteines 243 and 264.

Details

Redox score ?
87
PDB code
1l8r
Structure name
structure of the retinal determination protein dachshund reveals a dna-binding motif
Structure deposition date
2002-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
67
Minimum pKa ?
4
% buried
60
Peptide accession
Q9UI36
Residue number A
243
Residue number B
264
Peptide name
Dachshund homolog 1

Ligandability

Cysteine 243 of Dachshund homolog 1

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 264 of Dachshund homolog 1

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 Dachshund homolog 1 between cysteines 210 and 264.

Details

Redox score ?
83
PDB code
1l8r
Structure name
structure of the retinal determination protein dachshund reveals a dna-binding motif
Structure deposition date
2002-03-21
Thiol separation (Å)
4
Half-sphere exposure sum ?
79
Minimum pKa ?
4
% buried
72
Peptide accession
Q9UI36
Residue number A
210
Residue number B
264
Peptide name
Dachshund homolog 1

Ligandability

Cysteine 210 of Dachshund homolog 1

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 264 of Dachshund homolog 1

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 Dachshund homolog 1 between cysteines 188 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
1l8r
Structure name
structure of the retinal determination protein dachshund reveals a dna-binding motif
Structure deposition date
2002-03-21
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
45
Peptide accession
Q9UI36
Residue number A
188
Residue number B
243
Peptide name
Dachshund homolog 1

Ligandability

Cysteine 188 of Dachshund homolog 1

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 243 of Dachshund homolog 1

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 Dachshund homolog 1 between cysteines 210 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
1l8r
Structure name
structure of the retinal determination protein dachshund reveals a dna-binding motif
Structure deposition date
2002-03-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
76
Minimum pKa ?
16
% buried
68
Peptide accession
Q9UI36
Residue number A
210
Residue number B
243
Peptide name
Dachshund homolog 1

Ligandability

Cysteine 210 of Dachshund homolog 1

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 243 of Dachshund homolog 1

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 Dachshund homolog 1 between cysteines 188 and 210. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1l8r
Structure name
structure of the retinal determination protein dachshund reveals a dna-binding motif
Structure deposition date
2002-03-21
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
10
% buried
62
Peptide accession
Q9UI36
Residue number A
188
Residue number B
210
Peptide name
Dachshund homolog 1

Ligandability

Cysteine 188 of Dachshund homolog 1

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 210 of Dachshund homolog 1

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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