ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein DDI1 homolog 1

Intramolecular
Cysteine 272 and cysteine 276
Cysteine 248 and cysteine 272
Cysteine 316 and cysteine 340
Cysteine 248 and cysteine 276
Cysteine 248 and cysteine 316
A redox-regulated disulphide may form within Protein DDI1 homolog 1 between cysteines 272 and 276.

Details

Redox score ?
74
PDB code
3s8i
Structure name
the retroviral-like protease (rvp) domain of human ddi1
Structure deposition date
2011-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WTU0
Residue number A
272
Residue number B
276
Peptide name
Protein DDI1 homolog 1

Ligandability

Cysteine 272 of Protein DDI1 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 276 of Protein DDI1 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 Protein DDI1 homolog 1 between cysteines 248 and 272. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3s8i
Structure name
the retroviral-like protease (rvp) domain of human ddi1
Structure deposition date
2011-05-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WTU0
Residue number A
248
Residue number B
272
Peptide name
Protein DDI1 homolog 1

Ligandability

Cysteine 248 of Protein DDI1 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 272 of Protein DDI1 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 Protein DDI1 homolog 1 between cysteines 316 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
50
PDB code
3s8i
Structure name
the retroviral-like protease (rvp) domain of human ddi1
Structure deposition date
2011-05-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WTU0
Residue number A
316
Residue number B
340
Peptide name
Protein DDI1 homolog 1

Ligandability

Cysteine 316 of Protein DDI1 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 340 of Protein DDI1 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 Protein DDI1 homolog 1 between cysteines 248 and 276. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
3s8i
Structure name
the retroviral-like protease (rvp) domain of human ddi1
Structure deposition date
2011-05-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WTU0
Residue number A
248
Residue number B
276
Peptide name
Protein DDI1 homolog 1

Ligandability

Cysteine 248 of Protein DDI1 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 276 of Protein DDI1 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 Protein DDI1 homolog 1 between cysteines 248 and 316. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
3s8i
Structure name
the retroviral-like protease (rvp) domain of human ddi1
Structure deposition date
2011-05-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8WTU0
Residue number A
248
Residue number B
316
Peptide name
Protein DDI1 homolog 1

Ligandability

Cysteine 248 of Protein DDI1 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 316 of Protein DDI1 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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