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Ubiquitin-40S ribosomal protein S27a

Intramolecular
Cysteine 153 and cysteine 173
Cysteine 173 and cysteine 176
Cysteine 158 and cysteine 176
Cysteine 158 and cysteine 173
Cysteine 153 and cysteine 158
Cysteine 153 and cysteine 176
Cysteine 176 and cysteine 177
Cysteine 153 and cysteine 181
Cysteine 158 and cysteine 177
Cysteine 173 and cysteine 177
More...
Cysteine 177 and cysteine 181
Cysteine 173 and cysteine 181
Cysteine 153 and cysteine 177
Cysteine 176 and cysteine 181
A redox-regulated disulphide may form within Ubiquitin-40S ribosomal protein S27a between cysteines 153 and 173 (121 and 141 respectively in this structure).

Details

Redox score ?
93
PDB code
7syq
Structure name
structure of the wt ires and 40s ribosome ternary complex, open conformation
Structure deposition date
2021-11-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
35
Peptide accession
G1SK22
Residue number A
153
Residue number B
173
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 153 of Ubiquitin-40S ribosomal protein S27a

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 173 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 173 and 176 (141 and 144 respectively in this structure).

Details

Redox score ?
85
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)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
34
Peptide accession
G1SK22
Residue number A
173
Residue number B
176
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 173 of Ubiquitin-40S ribosomal protein S27a

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 176 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 158 and 176 (126 and 144 respectively in this structure).

Details

Redox score ?
84
PDB code
4kzz
Structure name
rabbit 40s ribosomal subunit in complex with mrna, initiator trna and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
8
% buried
30
Peptide accession
G1SK22
Residue number A
158
Residue number B
176
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 158 of Ubiquitin-40S ribosomal protein S27a

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 176 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 158 and 173 (126 and 141 respectively in this structure).

Details

Redox score ?
81
PDB code
4kzx
Structure name
rabbit 40s ribosomal subunit in complex with eif1
Structure deposition date
2013-05-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
8
% buried
48
Peptide accession
G1SK22
Residue number A
158
Residue number B
173
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 158 of Ubiquitin-40S ribosomal protein S27a

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 173 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 153 and 158 (121 and 126 respectively in this structure).

Details

Redox score ?
79
PDB code
4kzy
Structure name
rabbit 40s ribosomal subunit in complex with eif1 and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
34
Peptide accession
G1SK22
Residue number A
153
Residue number B
158
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 153 of Ubiquitin-40S ribosomal protein S27a

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 158 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 153 and 176 (121 and 144 respectively in this structure).

Details

Redox score ?
74
PDB code
4kzz
Structure name
rabbit 40s ribosomal subunit in complex with mrna, initiator trna and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
5
Half-sphere exposure sum ?
50
Minimum pKa ?
10
% buried
33
Peptide accession
G1SK22
Residue number A
153
Residue number B
176
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 153 of Ubiquitin-40S ribosomal protein S27a

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 176 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 176 and 177 (144 and 145 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
56
PDB code
4kzz
Structure name
rabbit 40s ribosomal subunit in complex with mrna, initiator trna and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
7
Half-sphere exposure sum ?
36
Minimum pKa ?
10
% buried
36
Peptide accession
G1SK22
Residue number A
176
Residue number B
177
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 176 of Ubiquitin-40S ribosomal protein S27a

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 177 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 153 and 181 (121 and 149 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
5k0y
Structure name
m48s late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eif2 ternary complex and eif3 i and g subunits relocated to the intersubunit face
Structure deposition date
2016-05-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
44
Peptide accession
G1SK22
Residue number A
153
Residue number B
181
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 153 of Ubiquitin-40S ribosomal protein S27a

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 181 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 158 and 177 (126 and 145 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
4kzy
Structure name
rabbit 40s ribosomal subunit in complex with eif1 and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
36
Minimum pKa ?
8
% buried
38
Peptide accession
G1SK22
Residue number A
158
Residue number B
177
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 158 of Ubiquitin-40S ribosomal protein S27a

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 177 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 173 and 177 (141 and 145 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
4kzz
Structure name
rabbit 40s ribosomal subunit in complex with mrna, initiator trna and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
9
Half-sphere exposure sum ?
43
Minimum pKa ?
10
% buried
53
Peptide accession
G1SK22
Residue number A
173
Residue number B
177
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 173 of Ubiquitin-40S ribosomal protein S27a

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 177 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 177 and 181 (145 and 149 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
5k0y
Structure name
m48s late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eif2 ternary complex and eif3 i and g subunits relocated to the intersubunit face
Structure deposition date
2016-05-17
Thiol separation (Å)
10
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
28
Peptide accession
G1SK22
Residue number A
177
Residue number B
181
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 177 of Ubiquitin-40S ribosomal protein S27a

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 181 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 173 and 181 (141 and 149 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
5k0y
Structure name
m48s late-stage initiation complex, purified from rabbit reticulocytes lysates, displaying eif2 ternary complex and eif3 i and g subunits relocated to the intersubunit face
Structure deposition date
2016-05-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
66
Peptide accession
G1SK22
Residue number A
173
Residue number B
181
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 173 of Ubiquitin-40S ribosomal protein S27a

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 181 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 153 and 177 (121 and 145 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
7sym
Structure name
structure of the hcv ires bound to the 40s ribosomal subunit, head opening
Structure deposition date
2021-11-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
10
% buried
nan
Peptide accession
G1SK22
Residue number A
153
Residue number B
177
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 153 of Ubiquitin-40S ribosomal protein S27a

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 177 of Ubiquitin-40S ribosomal protein S27a

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 Ubiquitin-40S ribosomal protein S27a between cysteines 176 and 181 (144 and 149 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
41
PDB code
4kzy
Structure name
rabbit 40s ribosomal subunit in complex with eif1 and eif1a
Structure deposition date
2013-05-30
Thiol separation (Å)
10
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
24
Peptide accession
G1SK22
Residue number A
176
Residue number B
181
Peptide name
Ubiquitin-40S ribosomal protein S27a

Ligandability

Cysteine 176 of Ubiquitin-40S ribosomal protein S27a

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 181 of Ubiquitin-40S ribosomal protein S27a

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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