ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Home
About
List

Ubiquitin-conjugating enzyme E2 E1

Intramolecular
Cysteine 122 and cysteine 159
Cysteine 67 and cysteine 153
Cysteine 122 and cysteine 131
A redox-regulated disulphide may form within Ubiquitin-conjugating enzyme E2 E1 between cysteines 122 and 159.

Details

Redox score ?
82
PDB code
6fga
Structure name
crystal structure of trim21 e3 ligase, ring domain in complex with its cognate e2 conjugating enzyme ube2e1
Structure deposition date
2018-01-10
Thiol separation (Å)
3
Half-sphere exposure sum ?
66
Minimum pKa ?
7
% buried
53
Peptide accession
P51965
Residue number A
122
Residue number B
159
Peptide name
Ubiquitin-conjugating enzyme E2 E1

Ligandability

Cysteine 122 of Ubiquitin-conjugating enzyme E2 E1

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 159 of Ubiquitin-conjugating enzyme E2 E1

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-conjugating enzyme E2 E1 between cysteines 67 and 153.

Details

Redox score ?
78
PDB code
5lbn
Structure name
high-resolution crystal structure of the ubc core domain of ube2e1/ubch6
Structure deposition date
2016-06-16
Thiol separation (Å)
3
Half-sphere exposure sum ?
61
Minimum pKa ?
9
% buried
62
Peptide accession
P51965
Residue number A
67
Residue number B
153
Peptide name
Ubiquitin-conjugating enzyme E2 E1

Ligandability

Cysteine 67 of Ubiquitin-conjugating enzyme E2 E1

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 153 of Ubiquitin-conjugating enzyme E2 E1

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-conjugating enzyme E2 E1 between cysteines 122 and 131. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
40
PDB code
6fga
Structure name
crystal structure of trim21 e3 ligase, ring domain in complex with its cognate e2 conjugating enzyme ube2e1
Structure deposition date
2018-01-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
66
Minimum pKa ?
11
% buried
32
Peptide accession
P51965
Residue number A
122
Residue number B
131
Peptide name
Ubiquitin-conjugating enzyme E2 E1

Ligandability

Cysteine 122 of Ubiquitin-conjugating enzyme E2 E1

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 131 of Ubiquitin-conjugating enzyme E2 E1

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.

If this tool was useful for finding a disulphide, please cite: