Splicing factor 3B subunit 3
Intermolecular
Cysteine 112 and cysteine 41 of Splicing factor 3B subunit 5
Cysteine 1244 of Splicing factor 3B subunit 1 and cysteine 1054 L
Intramolecular
Cysteine 508 and cysteine 547
Cysteine 589 and cysteine 641
Cysteine 410 and cysteine 427
Cysteine 547 and cysteine 589
Cysteine 251 and cysteine 289
Cysteine 289 and cysteine 340
7b92 A 112 B 41
A redox-regulated disulphide may form between cysteine 112 of Splicing factor 3B subunit 3 and cysteine 41 of Splicing factor 3B subunit 5. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
7b92
Structure name
structure of a minimal sf3b core in complex with sudemycin d6 (form ii)
Structure deposition date
2020-12-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
88
Minimum pKa ?
10
% buried
100
Peptide A name
Splicing factor 3B subunit 3
Peptide B name
Splicing factor 3B subunit 5
Peptide A accession
Q15393
Peptide B accession
Q9BWJ5
Peptide A residue number
112
Peptide B residue number
41
Ligandability
Cysteine 112 of Splicing factor 3B subunit 3
Cysteine 41 of Splicing factor 3B subunit 5
6ff4 u 1244 v 1054
A redox-regulated disulphide may form between cysteine 1244 of Splicing factor 3B subunit 1 and cysteine 1054 of Splicing factor 3B subunit 3. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
27
PDB code
6ff4
Structure name
human bact spliceosome core structure
Structure deposition date
2018-01-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
85
Minimum pKa ?
11
% buried
100
Peptide A name
Splicing factor 3B subunit 1
Peptide B name
Splicing factor 3B subunit 3
Peptide A accession
O75533
Peptide B accession
Q15393
Peptide A residue number
1244
Peptide B residue number
1054
Ligandability
Cysteine 1244 of Splicing factor 3B subunit 1
Cysteine 1054 of Splicing factor 3B subunit 3
5ife A 508 A 547
A redox-regulated disulphide may form within Splicing factor 3B subunit 3 between cysteines 508 and 547. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
5ife
Structure name
crystal structure of the human sf3b core complex
Structure deposition date
2016-02-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
Q15393
Residue number A
508
Residue number B
547
Peptide name
Splicing factor 3B subunit 3
Ligandability
Cysteine 508 of Splicing factor 3B subunit 3
Cysteine 547 of Splicing factor 3B subunit 3
8h7g A 589 A 641
A redox-regulated disulphide may form within Splicing factor 3B subunit 3 between cysteines 589 and 641. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
86
Peptide accession
Q15393
Residue number A
589
Residue number B
641
Peptide name
Splicing factor 3B subunit 3
Ligandability
Cysteine 589 of Splicing factor 3B subunit 3
Cysteine 641 of Splicing factor 3B subunit 3
7b92 A 410 A 427
A redox-regulated disulphide may form within Splicing factor 3B subunit 3 between cysteines 410 and 427. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
7b92
Structure name
structure of a minimal sf3b core in complex with sudemycin d6 (form ii)
Structure deposition date
2020-12-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
100
Peptide accession
Q15393
Residue number A
410
Residue number B
427
Peptide name
Splicing factor 3B subunit 3
Ligandability
Cysteine 410 of Splicing factor 3B subunit 3
Cysteine 427 of Splicing factor 3B subunit 3
8h7g A 547 A 589
A redox-regulated disulphide may form within Splicing factor 3B subunit 3 between cysteines 547 and 589. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
8h7g
Structure name
cryo-em structure of the human saga complex
Structure deposition date
2022-10-20
Thiol separation (Å)
10
Half-sphere exposure sum ?
72
Minimum pKa ?
11
% buried
90
Peptide accession
Q15393
Residue number A
547
Residue number B
589
Peptide name
Splicing factor 3B subunit 3
Ligandability
Cysteine 547 of Splicing factor 3B subunit 3
Cysteine 589 of Splicing factor 3B subunit 3
7omf A 251 A 289
A redox-regulated disulphide may form within Splicing factor 3B subunit 3 between cysteines 251 and 289. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
7omf
Structure name
structure of a minimal sf3b core in complex with sudemycin d6 (form i)
Structure deposition date
2021-05-21
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
Q15393
Residue number A
251
Residue number B
289
Peptide name
Splicing factor 3B subunit 3
Ligandability
Cysteine 251 of Splicing factor 3B subunit 3
Cysteine 289 of Splicing factor 3B subunit 3
7b0i A 289 A 340
A redox-regulated disulphide may form within Splicing factor 3B subunit 3 between cysteines 289 and 340. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
23
PDB code
7b0i
Structure name
structure of a minimal sf3b core in complex with spliceostatin a (form ii)
Structure deposition date
2020-11-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
79
Minimum pKa ?
12
% buried
100
Peptide accession
Q15393
Residue number A
289
Residue number B
340
Peptide name
Splicing factor 3B subunit 3
Ligandability
Cysteine 289 of Splicing factor 3B subunit 3
Cysteine 340 of Splicing factor 3B subunit 3
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