ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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(E3-independent) E2 ubiquitin-conjugating enzyme

Intramolecular
Cysteine 173 and cysteine 353
Cysteine 163 and cysteine 585
Cysteine 585 and cysteine 617
A redox-regulated disulphide may form within (E3-independent) E2 ubiquitin-conjugating enzyme between cysteines 173 and 353. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
51
PDB code
7un3
Structure name
complex of ube2o with nap1l1 and ubiquitylated ul2
Structure deposition date
2022-04-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
73
Minimum pKa ?
12
% buried
74
Peptide accession
Q9C0C9
Residue number A
173
Residue number B
353
Peptide name
(E3-independent) E2 ubiquitin-conjugating enzyme

Ligandability

Cysteine 173 of (E3-independent) E2 ubiquitin-conjugating enzyme

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 353 of (E3-independent) E2 ubiquitin-conjugating enzyme

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 (E3-independent) E2 ubiquitin-conjugating enzyme between cysteines 163 and 585. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
48
PDB code
7un3
Structure name
complex of ube2o with nap1l1 and ubiquitylated ul2
Structure deposition date
2022-04-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
Q9C0C9
Residue number A
163
Residue number B
585
Peptide name
(E3-independent) E2 ubiquitin-conjugating enzyme

Ligandability

Cysteine 163 of (E3-independent) E2 ubiquitin-conjugating enzyme

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 585 of (E3-independent) E2 ubiquitin-conjugating enzyme

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 (E3-independent) E2 ubiquitin-conjugating enzyme between cysteines 585 and 617. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
33
PDB code
7un6
Structure name
complex of ube2o with nap1l1
Structure deposition date
2022-04-09
Thiol separation (Å)
9
Half-sphere exposure sum ?
88
Minimum pKa ?
13
% buried
96
Peptide accession
Q9C0C9
Residue number A
585
Residue number B
617
Peptide name
(E3-independent) E2 ubiquitin-conjugating enzyme

Ligandability

Cysteine 585 of (E3-independent) E2 ubiquitin-conjugating enzyme

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 617 of (E3-independent) E2 ubiquitin-conjugating enzyme

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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