ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Transportin-3

Intermolecular
Cysteine 793 and cysteine 912
Intramolecular
Cysteine 634 and cysteine 672 L
Cysteine 296 and cysteine 330
Cysteine 663 and cysteine 699
Cysteine 908 and cysteine 912
Cysteine 585 and cysteine 634 L
Cysteine 841 and cysteine 842
Cysteine 662 and cysteine 663
Cysteine 187 and cysteine 204
Cysteine 296 and cysteine 303
More...
Cysteine 842 and cysteine 844
Cysteine 662 and cysteine 665
Cysteine 662 and cysteine 699
Cysteine 527 and cysteine 530
Cysteine 841 and cysteine 912
Cysteine 841 and cysteine 844
Cysteine 585 and cysteine 665
Cysteine 585 and cysteine 672
Cysteine 303 and cysteine 330
Cysteine 250 and cysteine 296
Cysteine 204 and cysteine 248
Cysteine 248 and cysteine 250
Cysteine 663 and cysteine 665
A redox-regulated disulphide may form between two units of Transportin-3 at cysteines 793 and 912. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4c0p
Structure name
unliganded transportin 3
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
67
Minimum pKa ?
10
% buried
78
Peptide A name
Transportin-3
Peptide B name
Transportin-3
Peptide A accession
Q9Y5L0
Peptide B accession
Q9Y5L0
Peptide A residue number
793
Peptide B residue number
912

Ligandability

Cysteine 793 of Transportin-3

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 912 of Transportin-3

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-3 between cysteines 634 and 672.

Details

Redox score ?
74
PDB code
6gx9
Structure name
crystal structure of the tnpo3 - cpsf6 rsld complex
Structure deposition date
2018-06-26
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
8
% buried
84
Peptide accession
Q9Y5L0
Residue number A
634
Residue number B
672
Peptide name
Transportin-3

Ligandability

Cysteine 634 of Transportin-3

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 672 of Transportin-3

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-3 between cysteines 296 and 330.

Details

Redox score ?
71
PDB code
4c0o
Structure name
transportin 3 in complex with phosphorylated asf/sf2
Structure deposition date
2013-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
87
Minimum pKa ?
8
% buried
98
Peptide accession
Q9Y5L0
Residue number A
296
Residue number B
330
Peptide name
Transportin-3

Ligandability

Cysteine 296 of Transportin-3

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 330 of Transportin-3

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-3 between cysteines 663 and 699.

Details

Redox score ?
66
PDB code
4c0p
Structure name
unliganded transportin 3
Structure deposition date
2013-08-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
78
Minimum pKa ?
9
% buried
96
Peptide accession
Q9Y5L0
Residue number A
663
Residue number B
699
Peptide name
Transportin-3

Ligandability

Cysteine 663 of Transportin-3

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 699 of Transportin-3

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-3 between cysteines 908 and 912. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
54
PDB code
4c0p
Structure name
unliganded transportin 3
Structure deposition date
2013-08-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
60
Minimum pKa ?
10
% buried
70
Peptide accession
Q9Y5L0
Residue number A
908
Residue number B
912
Peptide name
Transportin-3

Ligandability

Cysteine 908 of Transportin-3

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 912 of Transportin-3

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-3 between cysteines 585 and 634. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4ol0
Structure name
crystal structure of transportin-sr2, a karyopherin involved in human disease, in complex with ran
Structure deposition date
2014-01-23
Thiol separation (Å)
8
Half-sphere exposure sum ?
86
Minimum pKa ?
6
% buried
90
Peptide accession
Q9Y5L0
Residue number A
585
Residue number B
634
Peptide name
Transportin-3

Ligandability

Cysteine 585 of Transportin-3

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 634 of Transportin-3

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-3 between cysteines 841 and 842. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
4c0q
Structure name
transportin 3 in complex with ran(q69l)gtp
Structure deposition date
2013-08-06
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
12
% buried
85
Peptide accession
Q9Y5L0
Residue number A
841
Residue number B
842
Peptide name
Transportin-3

Ligandability

Cysteine 841 of Transportin-3

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 842 of Transportin-3

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-3 between cysteines 662 and 663. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4ol0
Structure name
crystal structure of transportin-sr2, a karyopherin involved in human disease, in complex with ran
Structure deposition date
2014-01-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
13
% buried
100
Peptide accession
Q9Y5L0
Residue number A
662
Residue number B
663
Peptide name
Transportin-3

Ligandability

Cysteine 662 of Transportin-3

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 663 of Transportin-3

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-3 between cysteines 187 and 204. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
6gx9
Structure name
crystal structure of the tnpo3 - cpsf6 rsld complex
Structure deposition date
2018-06-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
76
Minimum pKa ?
11
% buried
80
Peptide accession
Q9Y5L0
Residue number A
187
Residue number B
204
Peptide name
Transportin-3

Ligandability

Cysteine 187 of Transportin-3

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 204 of Transportin-3

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-3 between cysteines 296 and 303. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4c0o
Structure name
transportin 3 in complex with phosphorylated asf/sf2
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
8
% buried
100
Peptide accession
Q9Y5L0
Residue number A
296
Residue number B
303
Peptide name
Transportin-3

Ligandability

Cysteine 296 of Transportin-3

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 303 of Transportin-3

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-3 between cysteines 842 and 844. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
4c0o
Structure name
transportin 3 in complex with phosphorylated asf/sf2
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
54
Minimum pKa ?
11
% buried
59
Peptide accession
Q9Y5L0
Residue number A
842
Residue number B
844
Peptide name
Transportin-3

Ligandability

Cysteine 842 of Transportin-3

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-3

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-3 between cysteines 662 and 665. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
6gx9
Structure name
crystal structure of the tnpo3 - cpsf6 rsld complex
Structure deposition date
2018-06-26
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q9Y5L0
Residue number A
662
Residue number B
665
Peptide name
Transportin-3

Ligandability

Cysteine 662 of Transportin-3

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 665 of Transportin-3

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-3 between cysteines 662 and 699. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4c0p
Structure name
unliganded transportin 3
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
80
Minimum pKa ?
9
% buried
91
Peptide accession
Q9Y5L0
Residue number A
662
Residue number B
699
Peptide name
Transportin-3

Ligandability

Cysteine 662 of Transportin-3

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 699 of Transportin-3

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-3 between cysteines 527 and 530. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
4c0p
Structure name
unliganded transportin 3
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
82
Peptide accession
Q9Y5L0
Residue number A
527
Residue number B
530
Peptide name
Transportin-3

Ligandability

Cysteine 527 of Transportin-3

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 530 of Transportin-3

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-3 between cysteines 841 and 912. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
4c0q
Structure name
transportin 3 in complex with ran(q69l)gtp
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
88
Peptide accession
Q9Y5L0
Residue number A
841
Residue number B
912
Peptide name
Transportin-3

Ligandability

Cysteine 841 of Transportin-3

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 912 of Transportin-3

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-3 between cysteines 841 and 844. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
4c0q
Structure name
transportin 3 in complex with ran(q69l)gtp
Structure deposition date
2013-08-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
59
Minimum pKa ?
11
% buried
70
Peptide accession
Q9Y5L0
Residue number A
841
Residue number B
844
Peptide name
Transportin-3

Ligandability

Cysteine 841 of Transportin-3

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-3

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-3 between cysteines 585 and 665. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4c0p
Structure name
unliganded transportin 3
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
100
Peptide accession
Q9Y5L0
Residue number A
585
Residue number B
665
Peptide name
Transportin-3

Ligandability

Cysteine 585 of Transportin-3

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 665 of Transportin-3

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-3 between cysteines 585 and 672. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
4c0o
Structure name
transportin 3 in complex with phosphorylated asf/sf2
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
13
% buried
92
Peptide accession
Q9Y5L0
Residue number A
585
Residue number B
672
Peptide name
Transportin-3

Ligandability

Cysteine 585 of Transportin-3

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 672 of Transportin-3

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-3 between cysteines 303 and 330. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
4c0o
Structure name
transportin 3 in complex with phosphorylated asf/sf2
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
13
% buried
100
Peptide accession
Q9Y5L0
Residue number A
303
Residue number B
330
Peptide name
Transportin-3

Ligandability

Cysteine 303 of Transportin-3

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 330 of Transportin-3

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-3 between cysteines 250 and 296. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
4c0p
Structure name
unliganded transportin 3
Structure deposition date
2013-08-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
87
Minimum pKa ?
8
% buried
100
Peptide accession
Q9Y5L0
Residue number A
250
Residue number B
296
Peptide name
Transportin-3

Ligandability

Cysteine 250 of Transportin-3

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 296 of Transportin-3

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-3 between cysteines 204 and 248. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
4c0q
Structure name
transportin 3 in complex with ran(q69l)gtp
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
69
Minimum pKa ?
12
% buried
100
Peptide accession
Q9Y5L0
Residue number A
204
Residue number B
248
Peptide name
Transportin-3

Ligandability

Cysteine 204 of Transportin-3

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 248 of Transportin-3

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-3 between cysteines 248 and 250. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
29
PDB code
4c0q
Structure name
transportin 3 in complex with ran(q69l)gtp
Structure deposition date
2013-08-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
74
Minimum pKa ?
11
% buried
100
Peptide accession
Q9Y5L0
Residue number A
248
Residue number B
250
Peptide name
Transportin-3

Ligandability

Cysteine 248 of Transportin-3

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 250 of Transportin-3

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-3 between cysteines 663 and 665. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
24
PDB code
4c0p
Structure name
unliganded transportin 3
Structure deposition date
2013-08-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
13
% buried
100
Peptide accession
Q9Y5L0
Residue number A
663
Residue number B
665
Peptide name
Transportin-3

Ligandability

Cysteine 663 of Transportin-3

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 665 of Transportin-3

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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