ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Protein DDI1 homolog 2

Intramolecular
Cysteine 264 and cysteine 268
Cysteine 7 and cysteine 34
Cysteine 240 and cysteine 268
Cysteine 240 and cysteine 264
Cysteine 240 and cysteine 308
Cysteine 308 and cysteine 332
A redox-regulated disulphide may form within Protein DDI1 homolog 2 between cysteines 264 and 268 (232 and 236 respectively in this structure).

Details

Redox score ?
78
PDB code
4rgh
Structure name
human dna damage-inducible protein: from protein chemistry and 3d structure to deciphering its cellular role
Structure deposition date
2014-09-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
52
Peptide accession
Q5TDH0
Residue number A
264
Residue number B
268
Peptide name
Protein DDI1 homolog 2

Ligandability

Cysteine 264 of Protein DDI1 homolog 2

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 Protein DDI1 homolog 2

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 2 between cysteines 7 and 34 (107 and 134 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
60
PDB code
2n7d
Structure name
solution structure of the ubl domain of human ddi2
Structure deposition date
2015-09-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
44
Peptide accession
Q5TDH0
Residue number A
7
Residue number B
34
Peptide name
Protein DDI1 homolog 2

Ligandability

Cysteine 7 of Protein DDI1 homolog 2

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 34 of Protein DDI1 homolog 2

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 2 between cysteines 240 and 268 (208 and 236 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
4rgh
Structure name
human dna damage-inducible protein: from protein chemistry and 3d structure to deciphering its cellular role
Structure deposition date
2014-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
73
Peptide accession
Q5TDH0
Residue number A
240
Residue number B
268
Peptide name
Protein DDI1 homolog 2

Ligandability

Cysteine 240 of Protein DDI1 homolog 2

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 Protein DDI1 homolog 2

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 2 between cysteines 240 and 264 (208 and 232 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4rgh
Structure name
human dna damage-inducible protein: from protein chemistry and 3d structure to deciphering its cellular role
Structure deposition date
2014-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
80
Peptide accession
Q5TDH0
Residue number A
240
Residue number B
264
Peptide name
Protein DDI1 homolog 2

Ligandability

Cysteine 240 of Protein DDI1 homolog 2

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 Protein DDI1 homolog 2

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 2 between cysteines 240 and 308 (208 and 276 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
4rgh
Structure name
human dna damage-inducible protein: from protein chemistry and 3d structure to deciphering its cellular role
Structure deposition date
2014-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
63
Minimum pKa ?
12
% buried
92
Peptide accession
Q5TDH0
Residue number A
240
Residue number B
308
Peptide name
Protein DDI1 homolog 2

Ligandability

Cysteine 240 of Protein DDI1 homolog 2

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 308 of Protein DDI1 homolog 2

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 2 between cysteines 308 and 332 (276 and 300 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
4rgh
Structure name
human dna damage-inducible protein: from protein chemistry and 3d structure to deciphering its cellular role
Structure deposition date
2014-09-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
66
Minimum pKa ?
12
% buried
90
Peptide accession
Q5TDH0
Residue number A
308
Residue number B
332
Peptide name
Protein DDI1 homolog 2

Ligandability

Cysteine 308 of Protein DDI1 homolog 2

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 332 of Protein DDI1 homolog 2

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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