ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Importin subunit beta-1

Intermolecular
Cysteine 436 and cysteine 436 L
Cysteine 471 and cysteine 262 of Zinc finger protein SNAI1
Intramolecular
Cysteine 287 and cysteine 358 L
Cysteine 287 and cysteine 351
Cysteine 358 and cysteine 359 L
Cysteine 351 and cysteine 358 L
Cysteine 678 and cysteine 689 L
Cysteine 287 and cysteine 359 L
Cysteine 436 and cysteine 455 L
Cysteine 436 and cysteine 498 L
More...
Cysteine 498 and cysteine 543 L
Cysteine 118 and cysteine 158 L
Cysteine 351 and cysteine 359 L
Cysteine 351 and cysteine 392 L
Cysteine 345 and cysteine 392 L
A redox-regulated disulphide may form between two units of Importin subunit beta-1 at cysteines 436 and 436. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
1gcj
Structure name
n-terminal fragment of importin-beta
Structure deposition date
2000-07-31
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
100
Peptide A name
Importin subunit beta-1
Peptide B name
Importin subunit beta-1
Peptide A accession
P70168
Peptide B accession
P70168
Peptide A residue number
436
Peptide B residue number
436

Ligandability

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.

A redox-regulated disulphide may form between cysteine 471 of Importin subunit beta-1 and cysteine 262 of Zinc finger protein SNAI1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
3w5k
Structure name
crystal structure of snail1 and importin beta complex
Structure deposition date
2013-01-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
100
Peptide A name
Importin subunit beta-1
Peptide B name
Zinc finger protein SNAI1
Peptide A accession
Q14974
Peptide B accession
O95863
Peptide A residue number
471
Peptide B residue number
262

Ligandability

Cysteine 471 of Importin subunit beta-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 262 of Zinc finger protein SNAI1

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 subunit beta-1 between cysteines 287 and 358.

Details

Redox score ?
78
PDB code
2p8q
Structure name
crystal structure of human importin beta bound to the snurportin1 ibb- domain
Structure deposition date
2007-03-22
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
4
% buried
83
Peptide accession
Q14974
Residue number A
287
Residue number B
358
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 287 of Importin subunit beta-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 358 of Importin subunit beta-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.

A redox-regulated disulphide may form within Importin subunit beta-1 between cysteines 287 and 351.

Details

Redox score ?
63
PDB code
1m5n
Structure name
crystal structure of heat repeats (1-11) of importin b bound to the non-classical nls(67-94) of pthrp
Structure deposition date
2002-07-09
Thiol separation (Å)
5
Half-sphere exposure sum ?
84
Minimum pKa ?
8
% buried
100
Peptide accession
Q14974
Residue number A
287
Residue number B
351
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 287 of Importin subunit beta-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 351 of Importin subunit beta-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 Importin subunit beta-1 between cysteines 358 and 359.

Details

Redox score ?
62
PDB code
1ibr
Structure name
complex of ran with importin beta
Structure deposition date
1999-05-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
13
% buried
68
Peptide accession
Q14974
Residue number A
358
Residue number B
359
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 358 of Importin subunit beta-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 359 of Importin subunit beta-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.

A redox-regulated disulphide may form within Importin subunit beta-1 between cysteines 351 and 358. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
44
PDB code
1qgk
Structure name
structure of importin beta bound to the ibb domain of importin alpha
Structure deposition date
1999-04-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
4
% buried
84
Peptide accession
Q14974
Residue number A
351
Residue number B
358
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 351 of Importin subunit beta-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 358 of Importin subunit beta-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.

A redox-regulated disulphide may form within Importin subunit beta-1 between cysteines 678 and 689. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
3lww
Structure name
structure of an open and closed conformation of human importin beta bound to the snurportin1 ibb-domain trapped in the same crystallographic asymmetric unit
Structure deposition date
2010-02-24
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
87
Peptide accession
Q14974
Residue number A
678
Residue number B
689
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 678 of Importin subunit beta-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 689 of Importin subunit beta-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 Importin subunit beta-1 between cysteines 287 and 359. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
3lww
Structure name
structure of an open and closed conformation of human importin beta bound to the snurportin1 ibb-domain trapped in the same crystallographic asymmetric unit
Structure deposition date
2010-02-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
67
Peptide accession
Q14974
Residue number A
287
Residue number B
359
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 287 of Importin subunit beta-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 359 of Importin subunit beta-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.

A redox-regulated disulphide may form within Importin subunit beta-1 between cysteines 436 and 455. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
1m5n
Structure name
crystal structure of heat repeats (1-11) of importin b bound to the non-classical nls(67-94) of pthrp
Structure deposition date
2002-07-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
68
Peptide accession
Q14974
Residue number A
436
Residue number B
455
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 436 of Importin subunit beta-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 455 of Importin subunit beta-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 Importin subunit beta-1 between cysteines 436 and 498. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
1qgr
Structure name
structure of importin beta bound to the ibb domain of importin alpha (ii crystal form, grown at low ph)
Structure deposition date
1999-05-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
69
Minimum pKa ?
10
% buried
74
Peptide accession
Q14974
Residue number A
436
Residue number B
498
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 436 of Importin subunit beta-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 498 of Importin subunit beta-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 Importin subunit beta-1 between cysteines 498 and 543. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
3lww
Structure name
structure of an open and closed conformation of human importin beta bound to the snurportin1 ibb-domain trapped in the same crystallographic asymmetric unit
Structure deposition date
2010-02-24
Thiol separation (Å)
10
Half-sphere exposure sum ?
61
Minimum pKa ?
11
% buried
61
Peptide accession
Q14974
Residue number A
498
Residue number B
543
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 498 of Importin subunit beta-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 543 of Importin subunit beta-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 Importin subunit beta-1 between cysteines 118 and 158. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
3lww
Structure name
structure of an open and closed conformation of human importin beta bound to the snurportin1 ibb-domain trapped in the same crystallographic asymmetric unit
Structure deposition date
2010-02-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
12
% buried
100
Peptide accession
Q14974
Residue number A
118
Residue number B
158
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 118 of Importin subunit beta-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 158 of Importin subunit beta-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.

A redox-regulated disulphide may form within Importin subunit beta-1 between cysteines 351 and 359. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
2p8q
Structure name
crystal structure of human importin beta bound to the snurportin1 ibb- domain
Structure deposition date
2007-03-22
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
84
Peptide accession
Q14974
Residue number A
351
Residue number B
359
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 351 of Importin subunit beta-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 359 of Importin subunit beta-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.

A redox-regulated disulphide may form within Importin subunit beta-1 between cysteines 351 and 392. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
26
PDB code
1o6p
Structure name
importin beta bound to a glfg nucleoporin peptide
Structure deposition date
2002-10-10
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
Q14974
Residue number A
351
Residue number B
392
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 351 of Importin subunit beta-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 392 of Importin subunit beta-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.

A redox-regulated disulphide may form within Importin subunit beta-1 between cysteines 345 and 392. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
25
PDB code
1m5n
Structure name
crystal structure of heat repeats (1-11) of importin b bound to the non-classical nls(67-94) of pthrp
Structure deposition date
2002-07-09
Thiol separation (Å)
10
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
94
Peptide accession
Q14974
Residue number A
345
Residue number B
392
Peptide name
Importin subunit beta-1

Ligandability

Cysteine 345 of Importin subunit beta-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 392 of Importin subunit beta-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.

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