Importin-4
Intermolecular
Cysteine 95 and cysteine 114 of GTP-binding nuclear protein GSP1/CNR1
Cysteine 708 and cysteine 735 L
Intramolecular
Cysteine 250 and cysteine 270
Cysteine 726 and cysteine 782
Cysteine 725 and cysteine 782
Cysteine 269 and cysteine 270
Cysteine 732 and cysteine 735
Cysteine 732 and cysteine 782
Cysteine 864 and cysteine 870
Cysteine 566 and cysteine 567
More...Cysteine 459 and cysteine 483
Cysteine 725 and cysteine 726
Cysteine 677 and cysteine 708 L
Cysteine 222 and cysteine 269
8dyo A 95 B 114
A redox-regulated disulphide may form between cysteine 95 of Importin-4 and cysteine 114 of GTP-binding nuclear protein GSP1/CNR1. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
8dyo
Structure name
cryo-em structure of importin-4 bound to rangtp
Structure deposition date
2022-08-04
Thiol separation (Å)
8
Half-sphere exposure sum ?
53
Minimum pKa ?
10
% buried
38
Peptide A name
Importin-4
Peptide B name
GTP-binding nuclear protein GSP1/CNR1
Peptide A accession
Q8TEX9
Peptide B accession
P32835
Peptide A residue number
95
Peptide B residue number
114
Ligandability
Cysteine 95 of Importin-4
Cysteine 114 of GTP-binding nuclear protein GSP1/CNR1
5xah C 708 D 735
A redox-regulated disulphide may form between two units of Importin-4 at cysteines 708 and 735. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5xah
Structure name
crystal structure of human importin4
Structure deposition date
2017-03-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
22
Peptide A name
Importin-4
Peptide B name
Importin-4
Peptide A accession
Q8TEX9
Peptide B accession
Q8TEX9
Peptide A residue number
708
Peptide B residue number
735
Ligandability
Cysteine 708 of Importin-4
Cysteine 735 of Importin-4
8dyo A 250 A 270
A redox-regulated disulphide may form within Importin-4 between cysteines 250 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
8dyo
Structure name
cryo-em structure of importin-4 bound to rangtp
Structure deposition date
2022-08-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
90
Peptide accession
Q8TEX9
Residue number A
250
Residue number B
270
Peptide name
Importin-4
Ligandability
Cysteine 250 of Importin-4
Cysteine 270 of Importin-4
5xbk A 726 A 782
A redox-regulated disulphide may form within Importin-4 between cysteines 726 and 782. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
5xbk
Structure name
crystal structure of human importin4
Structure deposition date
2017-03-20
Thiol separation (Å)
6
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
70
Peptide accession
Q8TEX9
Residue number A
726
Residue number B
782
Peptide name
Importin-4
Ligandability
Cysteine 726 of Importin-4
Cysteine 782 of Importin-4
5xah D 725 D 782
A redox-regulated disulphide may form within Importin-4 between cysteines 725 and 782. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
5xah
Structure name
crystal structure of human importin4
Structure deposition date
2017-03-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
82
Peptide accession
Q8TEX9
Residue number A
725
Residue number B
782
Peptide name
Importin-4
Ligandability
Cysteine 725 of Importin-4
Cysteine 782 of Importin-4
8dyo A 269 A 270
A redox-regulated disulphide may form within Importin-4 between cysteines 269 and 270. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
8dyo
Structure name
cryo-em structure of importin-4 bound to rangtp
Structure deposition date
2022-08-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
65
Minimum pKa ?
11
% buried
84
Peptide accession
Q8TEX9
Residue number A
269
Residue number B
270
Peptide name
Importin-4
Ligandability
Cysteine 269 of Importin-4
Cysteine 270 of Importin-4
5xah D 732 D 735
A redox-regulated disulphide may form within Importin-4 between cysteines 732 and 735. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
5xah
Structure name
crystal structure of human importin4
Structure deposition date
2017-03-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
41
Minimum pKa ?
9
% buried
10
Peptide accession
Q8TEX9
Residue number A
732
Residue number B
735
Peptide name
Importin-4
Ligandability
Cysteine 732 of Importin-4
Cysteine 735 of Importin-4
5xbk C 732 C 782
A redox-regulated disulphide may form within Importin-4 between cysteines 732 and 782. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5xbk
Structure name
crystal structure of human importin4
Structure deposition date
2017-03-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
60
Minimum pKa ?
9
% buried
24
Peptide accession
Q8TEX9
Residue number A
732
Residue number B
782
Peptide name
Importin-4
Ligandability
Cysteine 732 of Importin-4
Cysteine 782 of Importin-4
5xbk C 864 C 870
A redox-regulated disulphide may form within Importin-4 between cysteines 864 and 870. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
5xbk
Structure name
crystal structure of human importin4
Structure deposition date
2017-03-20
Thiol separation (Å)
8
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
46
Peptide accession
Q8TEX9
Residue number A
864
Residue number B
870
Peptide name
Importin-4
Ligandability
Cysteine 864 of Importin-4
Cysteine 870 of Importin-4
7unk A 566 A 567
A redox-regulated disulphide may form within Importin-4 between cysteines 566 and 567. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7unk
Structure name
structure of importin-4 bound to the h3-h4-asf1 histone-histone chaperone complex
Structure deposition date
2022-04-11
Thiol separation (Å)
7
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
74
Peptide accession
Q8TEX9
Residue number A
566
Residue number B
567
Peptide name
Importin-4
Ligandability
Cysteine 566 of Importin-4
Cysteine 567 of Importin-4
7unk A 459 A 483
A redox-regulated disulphide may form within Importin-4 between cysteines 459 and 483. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7unk
Structure name
structure of importin-4 bound to the h3-h4-asf1 histone-histone chaperone complex
Structure deposition date
2022-04-11
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
10
% buried
82
Peptide accession
Q8TEX9
Residue number A
459
Residue number B
483
Peptide name
Importin-4
Ligandability
Cysteine 459 of Importin-4
Cysteine 483 of Importin-4
5xbk D 725 D 726
A redox-regulated disulphide may form within Importin-4 between cysteines 725 and 726. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
5xbk
Structure name
crystal structure of human importin4
Structure deposition date
2017-03-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
82
Minimum pKa ?
9
% buried
70
Peptide accession
Q8TEX9
Residue number A
725
Residue number B
726
Peptide name
Importin-4
Ligandability
Cysteine 725 of Importin-4
Cysteine 726 of Importin-4
7unk A 677 A 708
A redox-regulated disulphide may form within Importin-4 between cysteines 677 and 708. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
7unk
Structure name
structure of importin-4 bound to the h3-h4-asf1 histone-histone chaperone complex
Structure deposition date
2022-04-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
79
Minimum pKa ?
11
% buried
94
Peptide accession
Q8TEX9
Residue number A
677
Residue number B
708
Peptide name
Importin-4
Ligandability
Cysteine 677 of Importin-4
Cysteine 708 of Importin-4
8dyo A 222 A 269
A redox-regulated disulphide may form within Importin-4 between cysteines 222 and 269. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
8dyo
Structure name
cryo-em structure of importin-4 bound to rangtp
Structure deposition date
2022-08-04
Thiol separation (Å)
9
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
76
Peptide accession
Q8TEX9
Residue number A
222
Residue number B
269
Peptide name
Importin-4
Ligandability
Cysteine 222 of Importin-4
Cysteine 269 of Importin-4
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