ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase RNF13

Intermolecular
Cysteine 258 and cysteine 266
Cysteine 281 and cysteine 266
Cysteine 278 and cysteine 266
Cysteine 278 and cysteine 243
A redox-regulated disulphide may form between two units of E3 ubiquitin-protein ligase RNF13 at cysteines 258 and 266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
59
PDB code
5zc4
Structure name
crystal structure of rnf13 ring domain
Structure deposition date
2018-02-14
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
2
% buried
71
Peptide A name
E3 ubiquitin-protein ligase RNF13
Peptide B name
E3 ubiquitin-protein ligase RNF13
Peptide A accession
O43567
Peptide B accession
O43567
Peptide A residue number
258
Peptide B residue number
266

Ligandability

Cysteine 258 of E3 ubiquitin-protein ligase RNF13

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 266 of E3 ubiquitin-protein ligase RNF13

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 between two units of E3 ubiquitin-protein ligase RNF13 at cysteines 281 and 266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
47
PDB code
5zc4
Structure name
crystal structure of rnf13 ring domain
Structure deposition date
2018-02-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
64
Peptide A name
E3 ubiquitin-protein ligase RNF13
Peptide B name
E3 ubiquitin-protein ligase RNF13
Peptide A accession
O43567
Peptide B accession
O43567
Peptide A residue number
281
Peptide B residue number
266

Ligandability

Cysteine 281 of E3 ubiquitin-protein ligase RNF13

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 266 of E3 ubiquitin-protein ligase RNF13

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 between two units of E3 ubiquitin-protein ligase RNF13 at cysteines 278 and 266. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
36
PDB code
5zc4
Structure name
crystal structure of rnf13 ring domain
Structure deposition date
2018-02-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
74
Minimum pKa ?
14
% buried
80
Peptide A name
E3 ubiquitin-protein ligase RNF13
Peptide B name
E3 ubiquitin-protein ligase RNF13
Peptide A accession
O43567
Peptide B accession
O43567
Peptide A residue number
278
Peptide B residue number
266

Ligandability

Cysteine 278 of E3 ubiquitin-protein ligase RNF13

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 266 of E3 ubiquitin-protein ligase RNF13

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 between two units of E3 ubiquitin-protein ligase RNF13 at cysteines 278 and 243. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
35
PDB code
5zc4
Structure name
crystal structure of rnf13 ring domain
Structure deposition date
2018-02-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
78
Peptide A name
E3 ubiquitin-protein ligase RNF13
Peptide B name
E3 ubiquitin-protein ligase RNF13
Peptide A accession
O43567
Peptide B accession
O43567
Peptide A residue number
278
Peptide B residue number
243

Ligandability

Cysteine 278 of E3 ubiquitin-protein ligase RNF13

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 243 of E3 ubiquitin-protein ligase RNF13

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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