ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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RRP12-like protein

Intramolecular
Cysteine 799 and cysteine 839 L
Cysteine 288 and cysteine 326
Cysteine 261 and cysteine 317
Cysteine 288 and cysteine 317
Cysteine 865 and cysteine 919
Cysteine 261 and cysteine 288
A redox-regulated disulphide may form within RRP12-like protein between cysteines 799 and 839.

Details

Redox score ?
67
PDB code
7wtz
Structure name
cryo-em structure of a human pre-40s ribosomal subunit - state rrp12- b2
Structure deposition date
2022-02-05
Thiol separation (Å)
4
Half-sphere exposure sum ?
74
Minimum pKa ?
8
% buried
99
Peptide accession
Q5JTH9
Residue number A
799
Residue number B
839
Peptide name
RRP12-like protein

Ligandability

Cysteine 799 of RRP12-like 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 839 of RRP12-like 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.

Ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within RRP12-like protein between cysteines 288 and 326. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
45
PDB code
7wtu
Structure name
cryo-em structure of a human pre-40s ribosomal subunit - state rrp12- a1 (without ck1)
Structure deposition date
2022-02-05
Thiol separation (Å)
7
Half-sphere exposure sum ?
80
Minimum pKa ?
12
% buried
95
Peptide accession
Q5JTH9
Residue number A
288
Residue number B
326
Peptide name
RRP12-like protein

Ligandability

Cysteine 288 of RRP12-like 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 326 of RRP12-like 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 RRP12-like protein between cysteines 261 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
43
PDB code
7wtx
Structure name
cryo-em structure of a human pre-40s ribosomal subunit - state rrp12- b1
Structure deposition date
2022-02-05
Thiol separation (Å)
8
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
58
Peptide accession
Q5JTH9
Residue number A
261
Residue number B
317
Peptide name
RRP12-like protein

Ligandability

Cysteine 261 of RRP12-like 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 317 of RRP12-like 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 RRP12-like protein between cysteines 288 and 317. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
32
PDB code
7wtv
Structure name
cryo-em structure of a human pre-40s ribosomal subunit - state rrp12- a2
Structure deposition date
2022-02-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
10
% buried
77
Peptide accession
Q5JTH9
Residue number A
288
Residue number B
317
Peptide name
RRP12-like protein

Ligandability

Cysteine 288 of RRP12-like 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 317 of RRP12-like 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 RRP12-like protein between cysteines 865 and 919. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
31
PDB code
7wtv
Structure name
cryo-em structure of a human pre-40s ribosomal subunit - state rrp12- a2
Structure deposition date
2022-02-05
Thiol separation (Å)
9
Half-sphere exposure sum ?
87
Minimum pKa ?
11
% buried
100
Peptide accession
Q5JTH9
Residue number A
865
Residue number B
919
Peptide name
RRP12-like protein

Ligandability

Cysteine 865 of RRP12-like 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 919 of RRP12-like 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 RRP12-like protein between cysteines 261 and 288. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
7wtx
Structure name
cryo-em structure of a human pre-40s ribosomal subunit - state rrp12- b1
Structure deposition date
2022-02-05
Thiol separation (Å)
10
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
77
Peptide accession
Q5JTH9
Residue number A
261
Residue number B
288
Peptide name
RRP12-like protein

Ligandability

Cysteine 261 of RRP12-like 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 288 of RRP12-like 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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