ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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40S ribosomal protein S14

Intramolecular
Cysteine 71 and cysteine 102
Cysteine 48 and cysteine 102
Cysteine 48 and cysteine 71
A redox-regulated disulphide may form within 40S ribosomal protein S14 between cysteines 71 and 102 (54 and 85 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
57
PDB code
4kzy
Structure name
rabbit 40s ribosomal subunit in complex with eif1 and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
72
Minimum pKa ?
12
% buried
92
Peptide accession
G1U472
Residue number A
71
Residue number B
102
Peptide name
40S ribosomal protein S14

Ligandability

Cysteine 71 of 40S ribosomal protein S14

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 102 of 40S ribosomal protein S14

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 40S ribosomal protein S14 between cysteines 48 and 102 (31 and 85 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
4kzy
Structure name
rabbit 40s ribosomal subunit in complex with eif1 and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
13
% buried
100
Peptide accession
G1U472
Residue number A
48
Residue number B
102
Peptide name
40S ribosomal protein S14

Ligandability

Cysteine 48 of 40S ribosomal protein S14

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 102 of 40S ribosomal protein S14

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 40S ribosomal protein S14 between cysteines 48 and 71 (31 and 54 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
7syn
Structure name
structure of the hcv ires bound to the 40s ribosomal subunit, head opening
Structure deposition date
2021-11-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
98
Peptide accession
G1U472
Residue number A
48
Residue number B
71
Peptide name
40S ribosomal protein S14

Ligandability

Cysteine 48 of 40S ribosomal protein S14

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 71 of 40S ribosomal protein S14

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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