ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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U5 small nuclear ribonucleoprotein 40 kDa protein

Intramolecular
Cysteine 71 and cysteine 72
Cysteine 71 and cysteine 157
Cysteine 157 and cysteine 168
A redox-regulated disulphide may form within U5 small nuclear ribonucleoprotein 40 kDa protein between cysteines 71 and 72. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
34
PDB code
6id0
Structure name
cryo-em structure of a human intron lariat spliceosome prior to prp43 loaded (ils1 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
99
Minimum pKa ?
14
% buried
100
Peptide accession
Q96DI7
Residue number A
71
Residue number B
72
Peptide name
U5 small nuclear ribonucleoprotein 40 kDa protein

Ligandability

Cysteine 71 of U5 small nuclear ribonucleoprotein 40 kDa protein

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 72 of U5 small nuclear ribonucleoprotein 40 kDa protein

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 U5 small nuclear ribonucleoprotein 40 kDa protein between cysteines 71 and 157. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
27
PDB code
6id1
Structure name
cryo-em structure of a human intron lariat spliceosome after prp43 loaded (ils2 complex) at 2
Structure deposition date
2018-09-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
104
Minimum pKa ?
14
% buried
100
Peptide accession
Q96DI7
Residue number A
71
Residue number B
157
Peptide name
U5 small nuclear ribonucleoprotein 40 kDa protein

Ligandability

Cysteine 71 of U5 small nuclear ribonucleoprotein 40 kDa protein

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 157 of U5 small nuclear ribonucleoprotein 40 kDa protein

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 U5 small nuclear ribonucleoprotein 40 kDa protein between cysteines 157 and 168. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
23
PDB code
7w59
Structure name
the cryo-em structure of human pre-c*-i complex
Structure deposition date
2021-11-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
98
Minimum pKa ?
13
% buried
100
Peptide accession
Q96DI7
Residue number A
157
Residue number B
168
Peptide name
U5 small nuclear ribonucleoprotein 40 kDa protein

Ligandability

Cysteine 157 of U5 small nuclear ribonucleoprotein 40 kDa protein

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 168 of U5 small nuclear ribonucleoprotein 40 kDa protein

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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