ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Probable E3 ubiquitin-protein ligase MID2

Intramolecular
Cysteine 195 and cysteine 218
Cysteine 195 and cysteine 215
Cysteine 215 and cysteine 218
Cysteine 207 and cysteine 218
A redox-regulated disulphide may form within Probable E3 ubiquitin-protein ligase MID2 between cysteines 195 and 218 (21 and 44 respectively in this structure).

Details

Redox score ?
87
PDB code
2dja
Structure name
solution structure of the b-box domain of the human midline-2 protein
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
10
Peptide accession
Q9UJV3
Residue number A
195
Residue number B
218
Peptide name
Probable E3 ubiquitin-protein ligase MID2

Ligandability

Cysteine 195 of Probable E3 ubiquitin-protein ligase MID2

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 218 of Probable E3 ubiquitin-protein ligase MID2

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 Probable E3 ubiquitin-protein ligase MID2 between cysteines 195 and 215 (21 and 41 respectively in this structure).

Details

Redox score ?
84
PDB code
2dja
Structure name
solution structure of the b-box domain of the human midline-2 protein
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
8
Peptide accession
Q9UJV3
Residue number A
195
Residue number B
215
Peptide name
Probable E3 ubiquitin-protein ligase MID2

Ligandability

Cysteine 195 of Probable E3 ubiquitin-protein ligase MID2

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 215 of Probable E3 ubiquitin-protein ligase MID2

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 Probable E3 ubiquitin-protein ligase MID2 between cysteines 215 and 218 (41 and 44 respectively in this structure).

Details

Redox score ?
75
PDB code
2dja
Structure name
solution structure of the b-box domain of the human midline-2 protein
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
9
% buried
10
Peptide accession
Q9UJV3
Residue number A
215
Residue number B
218
Peptide name
Probable E3 ubiquitin-protein ligase MID2

Ligandability

Cysteine 215 of Probable E3 ubiquitin-protein ligase MID2

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 218 of Probable E3 ubiquitin-protein ligase MID2

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 Probable E3 ubiquitin-protein ligase MID2 between cysteines 207 and 218 (33 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
49
PDB code
2dja
Structure name
solution structure of the b-box domain of the human midline-2 protein
Structure deposition date
2006-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
6
Peptide accession
Q9UJV3
Residue number A
207
Residue number B
218
Peptide name
Probable E3 ubiquitin-protein ligase MID2

Ligandability

Cysteine 207 of Probable E3 ubiquitin-protein ligase MID2

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 218 of Probable E3 ubiquitin-protein ligase MID2

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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