ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Importin-13

Intramolecular
Cysteine 848 and cysteine 896
Cysteine 309 and cysteine 343
Cysteine 838 and cysteine 884
Cysteine 198 and cysteine 239
Cysteine 163 and cysteine 217 L
Cysteine 555 and cysteine 558
Cysteine 198 and cysteine 225
A redox-regulated disulphide may form within Importin-13 between cysteines 848 and 896.

Details

Redox score ?
75
PDB code
2x19
Structure name
crystal structure of importin13 - rangtp complex
Structure deposition date
2009-12-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
59
Minimum pKa ?
7
% buried
62
Peptide accession
O94829
Residue number A
848
Residue number B
896
Peptide name
Importin-13

Ligandability

Cysteine 848 of Importin-13

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 896 of Importin-13

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 Importin-13 between cysteines 309 and 343.

Details

Redox score ?
70
PDB code
2x19
Structure name
crystal structure of importin13 - rangtp complex
Structure deposition date
2009-12-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
98
Peptide accession
O94829
Residue number A
309
Residue number B
343
Peptide name
Importin-13

Ligandability

Cysteine 309 of Importin-13

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 343 of Importin-13

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 Importin-13 between cysteines 838 and 884.

Details

Redox score ?
66
PDB code
2x19
Structure name
crystal structure of importin13 - rangtp complex
Structure deposition date
2009-12-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
74
Minimum pKa ?
7
% buried
82
Peptide accession
O94829
Residue number A
838
Residue number B
884
Peptide name
Importin-13

Ligandability

Cysteine 838 of Importin-13

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 884 of Importin-13

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 Importin-13 between cysteines 198 and 239. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
2x19
Structure name
crystal structure of importin13 - rangtp complex
Structure deposition date
2009-12-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
70
Minimum pKa ?
12
% buried
66
Peptide accession
O94829
Residue number A
198
Residue number B
239
Peptide name
Importin-13

Ligandability

Cysteine 198 of Importin-13

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 239 of Importin-13

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 Importin-13 between cysteines 163 and 217. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
46
PDB code
2x19
Structure name
crystal structure of importin13 - rangtp complex
Structure deposition date
2009-12-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
9
% buried
22
Peptide accession
O94829
Residue number A
163
Residue number B
217
Peptide name
Importin-13

Ligandability

Cysteine 163 of Importin-13

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 217 of Importin-13

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Ligandable in the dataset of Backus et al.

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 Importin-13 between cysteines 555 and 558. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
42
PDB code
2x19
Structure name
crystal structure of importin13 - rangtp complex
Structure deposition date
2009-12-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
75
Minimum pKa ?
12
% buried
82
Peptide accession
O94829
Residue number A
555
Residue number B
558
Peptide name
Importin-13

Ligandability

Cysteine 555 of Importin-13

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 558 of Importin-13

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 Importin-13 between cysteines 198 and 225. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2x19
Structure name
crystal structure of importin13 - rangtp complex
Structure deposition date
2009-12-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
78
Peptide accession
O94829
Residue number A
198
Residue number B
225
Peptide name
Importin-13

Ligandability

Cysteine 198 of Importin-13

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 225 of Importin-13

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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