ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Splicing factor U2AF 65 kDa subunit

Intramolecular
Cysteine 379 and cysteine 464 L
Cysteine 442 and cysteine 464 L
Cysteine 406 and cysteine 442
Cysteine 379 and cysteine 442
A redox-regulated disulphide may form within Splicing factor U2AF 65 kDa subunit between cysteines 379 and 464. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7sn6
Structure name
u2af65 uhm bound to sf3b155 ulm5
Structure deposition date
2021-10-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
74
Peptide accession
P26368
Residue number A
379
Residue number B
464
Peptide name
Splicing factor U2AF 65 kDa subunit

Ligandability

Cysteine 379 of Splicing factor U2AF 65 kDa subunit

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 464 of Splicing factor U2AF 65 kDa subunit

Not ligandable in the dataset of Yang et al.

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Splicing factor U2AF 65 kDa subunit between cysteines 442 and 464. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
7sn6
Structure name
u2af65 uhm bound to sf3b155 ulm5
Structure deposition date
2021-10-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
72
Minimum pKa ?
9
% buried
52
Peptide accession
P26368
Residue number A
442
Residue number B
464
Peptide name
Splicing factor U2AF 65 kDa subunit

Ligandability

Cysteine 442 of Splicing factor U2AF 65 kDa subunit

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 464 of Splicing factor U2AF 65 kDa subunit

Not ligandable in the dataset of Yang et al.

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.

Ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Splicing factor U2AF 65 kDa subunit between cysteines 406 and 442. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7sn6
Structure name
u2af65 uhm bound to sf3b155 ulm5
Structure deposition date
2021-10-27
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
12
% buried
82
Peptide accession
P26368
Residue number A
406
Residue number B
442
Peptide name
Splicing factor U2AF 65 kDa subunit

Ligandability

Cysteine 406 of Splicing factor U2AF 65 kDa subunit

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 442 of Splicing factor U2AF 65 kDa subunit

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 Splicing factor U2AF 65 kDa subunit between cysteines 379 and 442. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
2m0g
Structure name
structure, phosphorylation and u2af65 binding of the nterminal domain of splicing factor 1 during 3 splice site recognition
Structure deposition date
2012-10-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
84
Peptide accession
P26368
Residue number A
379
Residue number B
442
Peptide name
Splicing factor U2AF 65 kDa subunit

Ligandability

Cysteine 379 of Splicing factor U2AF 65 kDa subunit

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 442 of Splicing factor U2AF 65 kDa subunit

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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