ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transportin-1

Intramolecular
Cysteine 285 and cysteine 386
Cysteine 164 and cysteine 205 L
Cysteine 142 and cysteine 164 L
Cysteine 826 and cysteine 862 L
Cysteine 142 and cysteine 205 L
Cysteine 806 and cysteine 844
Cysteine 205 and cysteine 244 L
Cysteine 826 and cysteine 844
Cysteine 806 and cysteine 826
Cysteine 467 and cysteine 509 L
A redox-regulated disulphide may form within Transportin-1 between cysteines 285 and 386 (277 and 378 respectively in this structure).

Details

Redox score ?
70
PDB code
7cyl
Structure name
crystal structure of karyopherin-beta2 in complex with fus py- nls(p525l)
Structure deposition date
2020-09-03
Thiol separation (Å)
4
Half-sphere exposure sum ?
83
Minimum pKa ?
8
% buried
93
Peptide accession
Q92973
Residue number A
285
Residue number B
386
Peptide name
Transportin-1

Ligandability

Cysteine 285 of Transportin-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 386 of Transportin-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 Transportin-1 between cysteines 164 and 205 (156 and 197 respectively in this structure).

Details

Redox score ?
67
PDB code
2h4m
Structure name
karyopherin beta2/transportin-m9nls
Structure deposition date
2006-05-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
9
% buried
100
Peptide accession
Q92973
Residue number A
164
Residue number B
205
Peptide name
Transportin-1

Ligandability

Cysteine 164 of Transportin-1

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 205 of Transportin-1

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 Transportin-1 between cysteines 142 and 164 (134 and 156 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
5tqc
Structure name
crystal structure of transport factor karyopherin-beta 2 in complex with the py-nls of ribosomal protein l4 (rpl4)
Structure deposition date
2016-10-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
65
Minimum pKa ?
9
% buried
83
Peptide accession
Q92973
Residue number A
142
Residue number B
164
Peptide name
Transportin-1

Ligandability

Cysteine 142 of Transportin-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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 164 of Transportin-1

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 Transportin-1 between cysteines 826 and 862 (818 and 854 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
7cyl
Structure name
crystal structure of karyopherin-beta2 in complex with fus py- nls(p525l)
Structure deposition date
2020-09-03
Thiol separation (Å)
9
Half-sphere exposure sum ?
64
Minimum pKa ?
10
% buried
60
Peptide accession
Q92973
Residue number A
826
Residue number B
862
Peptide name
Transportin-1

Ligandability

Cysteine 826 of Transportin-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 862 of Transportin-1

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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Transportin-1 between cysteines 142 and 205 (134 and 197 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4oo6
Structure name
crystal structure of human kap-beta2 bound to the nls of hcc1 (hepato cellular carcinoma protein 1)
Structure deposition date
2014-01-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
88
Peptide accession
Q92973
Residue number A
142
Residue number B
205
Peptide name
Transportin-1

Ligandability

Cysteine 142 of Transportin-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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 205 of Transportin-1

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 Transportin-1 between cysteines 806 and 844 (798 and 836 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
2h4m
Structure name
karyopherin beta2/transportin-m9nls
Structure deposition date
2006-05-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
95
Peptide accession
Q92973
Residue number A
806
Residue number B
844
Peptide name
Transportin-1

Ligandability

Cysteine 806 of Transportin-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 844 of Transportin-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 Transportin-1 between cysteines 205 and 244 (197 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 ?
31
PDB code
1qbk
Structure name
structure of the karyopherin beta2-ran gppnhp nuclear transport complex
Structure deposition date
1999-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
12
% buried
86
Peptide accession
Q92973
Residue number A
205
Residue number B
244
Peptide name
Transportin-1

Ligandability

Cysteine 205 of Transportin-1

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 244 of Transportin-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 Transportin-1 between cysteines 826 and 844 (818 and 836 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
2qmr
Structure name
karyopherin beta2/transportin
Structure deposition date
2007-07-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
99
Peptide accession
Q92973
Residue number A
826
Residue number B
844
Peptide name
Transportin-1

Ligandability

Cysteine 826 of Transportin-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 844 of Transportin-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 Transportin-1 between cysteines 806 and 826 (798 and 818 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
5j3v
Structure name
crystal structure of human karyopherin-beta2 bound to the histone h3 tail
Structure deposition date
2016-03-31
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
13
% buried
100
Peptide accession
Q92973
Residue number A
806
Residue number B
826
Peptide name
Transportin-1

Ligandability

Cysteine 806 of Transportin-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 826 of Transportin-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 Transportin-1 between cysteines 467 and 509 (459 and 501 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
22
PDB code
4fdd
Structure name
crystal structure of kap beta2-py-nls
Structure deposition date
2012-05-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
101
Minimum pKa ?
13
% buried
100
Peptide accession
Q92973
Residue number A
467
Residue number B
509
Peptide name
Transportin-1

Ligandability

Cysteine 467 of Transportin-1

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.

Ligandable in the dataset of Kuljanin et al.

Cysteine 509 of Transportin-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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