ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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U3 small nucleolar RNA-associated protein 15 homolog

Intramolecular
Cysteine 253 and cysteine 255
Cysteine 85 and cysteine 169
Cysteine 169 and cysteine 171
A redox-regulated disulphide may form within U3 small nucleolar RNA-associated protein 15 homolog between cysteines 253 and 255. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
39
PDB code
7ruo
Structure name
crystal structure of human utp15
Structure deposition date
2021-08-17
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8TED0
Residue number A
253
Residue number B
255
Peptide name
U3 small nucleolar RNA-associated protein 15 homolog

Ligandability

Cysteine 253 of U3 small nucleolar RNA-associated protein 15 homolog

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 255 of U3 small nucleolar RNA-associated protein 15 homolog

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 U3 small nucleolar RNA-associated protein 15 homolog between cysteines 85 and 169. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7ruo
Structure name
crystal structure of human utp15
Structure deposition date
2021-08-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8TED0
Residue number A
85
Residue number B
169
Peptide name
U3 small nucleolar RNA-associated protein 15 homolog

Ligandability

Cysteine 85 of U3 small nucleolar RNA-associated protein 15 homolog

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 169 of U3 small nucleolar RNA-associated protein 15 homolog

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 U3 small nucleolar RNA-associated protein 15 homolog between cysteines 169 and 171. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
30
PDB code
7ruo
Structure name
crystal structure of human utp15
Structure deposition date
2021-08-17
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q8TED0
Residue number A
169
Residue number B
171
Peptide name
U3 small nucleolar RNA-associated protein 15 homolog

Ligandability

Cysteine 169 of U3 small nucleolar RNA-associated protein 15 homolog

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 171 of U3 small nucleolar RNA-associated protein 15 homolog

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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