ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

Intramolecular
Cysteine 378 and cysteine 430
Cysteine 284 and cysteine 286
Cysteine 373 and cysteine 378
A redox-regulated disulphide may form within tRNA-dihydrouridine(20) synthase [NAD(P)+]-like between cysteines 378 and 430. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
53
PDB code
5oc6
Structure name
crystal structure of human trna-dihydrouridine(20) synthase dsrbd in complex with a 22 nucleotide dsrna
Structure deposition date
2017-06-29
Thiol separation (Å)
6
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
56
Peptide accession
Q9NX74
Residue number A
378
Residue number B
430
Peptide name
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

Ligandability

Cysteine 378 of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

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 430 of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

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 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like between cysteines 284 and 286. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
6eza
Structure name
crystal structure of human trna-dihydrouridine(20) synthase catalytic domain e294k mutant
Structure deposition date
2017-11-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
72
Peptide accession
Q9NX74
Residue number A
284
Residue number B
286
Peptide name
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

Ligandability

Cysteine 284 of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

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 286 of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

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 tRNA-dihydrouridine(20) synthase [NAD(P)+]-like between cysteines 373 and 378. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
38
PDB code
1whn
Structure name
solution structure of the dsrbd from hypothetical protein bab26260
Structure deposition date
2004-05-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
52
Minimum pKa ?
10
% buried
26
Peptide accession
Q9D7B1
Residue number A
373
Residue number B
378
Peptide name
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

Ligandability

Cysteine 373 of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

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 378 of tRNA-dihydrouridine(20) synthase [NAD(P)+]-like

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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