ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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E3 ubiquitin-protein ligase AMFR

Intramolecular
Cysteine 356 and cysteine 378
Cysteine 375 and cysteine 378
Cysteine 341 and cysteine 344
Cysteine 356 and cysteine 375
Cysteine 341 and cysteine 364
Cysteine 344 and cysteine 364
A redox-regulated disulphide may form within E3 ubiquitin-protein ligase AMFR between cysteines 356 and 378.

Details

Redox score ?
89
PDB code
4lad
Structure name
crystal structure of the ube2g2:ring-g2br complex
Structure deposition date
2013-06-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
33
Minimum pKa ?
6
% buried
0
Peptide accession
Q9UKV5
Residue number A
356
Residue number B
378
Peptide name
E3 ubiquitin-protein ligase AMFR

Ligandability

Cysteine 356 of E3 ubiquitin-protein ligase AMFR

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 E3 ubiquitin-protein ligase AMFR

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 ubiquitin-protein ligase AMFR between cysteines 375 and 378.

Details

Redox score ?
88
PDB code
4lad
Structure name
crystal structure of the ube2g2:ring-g2br complex
Structure deposition date
2013-06-19
Thiol separation (Å)
3
Half-sphere exposure sum ?
47
Minimum pKa ?
6
% buried
4
Peptide accession
Q9UKV5
Residue number A
375
Residue number B
378
Peptide name
E3 ubiquitin-protein ligase AMFR

Ligandability

Cysteine 375 of E3 ubiquitin-protein ligase AMFR

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 E3 ubiquitin-protein ligase AMFR

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 ubiquitin-protein ligase AMFR between cysteines 341 and 344.

Details

Redox score ?
86
PDB code
4lad
Structure name
crystal structure of the ube2g2:ring-g2br complex
Structure deposition date
2013-06-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
19
Minimum pKa ?
8
% buried
0
Peptide accession
Q9UKV5
Residue number A
341
Residue number B
344
Peptide name
E3 ubiquitin-protein ligase AMFR

Ligandability

Cysteine 341 of E3 ubiquitin-protein ligase AMFR

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 344 of E3 ubiquitin-protein ligase AMFR

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 ubiquitin-protein ligase AMFR between cysteines 356 and 375.

Details

Redox score ?
84
PDB code
4lad
Structure name
crystal structure of the ube2g2:ring-g2br complex
Structure deposition date
2013-06-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
8
% buried
4
Peptide accession
Q9UKV5
Residue number A
356
Residue number B
375
Peptide name
E3 ubiquitin-protein ligase AMFR

Ligandability

Cysteine 356 of E3 ubiquitin-protein ligase AMFR

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 375 of E3 ubiquitin-protein ligase AMFR

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 ubiquitin-protein ligase AMFR between cysteines 341 and 364.

Details

Redox score ?
83
PDB code
2lxh
Structure name
nmr structure of the ring domain in ubiquitin ligase gp78
Structure deposition date
2012-08-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
7
% buried
14
Peptide accession
Q9UKV5
Residue number A
341
Residue number B
364
Peptide name
E3 ubiquitin-protein ligase AMFR

Ligandability

Cysteine 341 of E3 ubiquitin-protein ligase AMFR

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 364 of E3 ubiquitin-protein ligase AMFR

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 ubiquitin-protein ligase AMFR between cysteines 344 and 364.

Details

Redox score ?
80
PDB code
2lxh
Structure name
nmr structure of the ring domain in ubiquitin ligase gp78
Structure deposition date
2012-08-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
6
Peptide accession
Q9UKV5
Residue number A
344
Residue number B
364
Peptide name
E3 ubiquitin-protein ligase AMFR

Ligandability

Cysteine 344 of E3 ubiquitin-protein ligase AMFR

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 364 of E3 ubiquitin-protein ligase AMFR

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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