ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-type lectin domain family 4 member E

Intramolecular
Cysteine 80 and cysteine 91
Cysteine 108 and cysteine 205
Cysteine 179 and cysteine 197
Cysteine 79 and cysteine 80
Cysteine 79 and cysteine 91
A redox-regulated disulphide may form within C-type lectin domain family 4 member E between cysteines 80 and 91.

Details

Redox score ?
86
PDB code
3wh2
Structure name
human mincle in complex with citrate
Structure deposition date
2013-08-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9ULY5
Residue number A
80
Residue number B
91
Peptide name
C-type lectin domain family 4 member E

Ligandability

Cysteine 80 of C-type lectin domain family 4 member E

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 91 of C-type lectin domain family 4 member E

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 C-type lectin domain family 4 member E between cysteines 108 and 205.

Details

Redox score ?
83
PDB code
3wh3
Structure name
human mincle, ligand free form
Structure deposition date
2013-08-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9ULY5
Residue number A
108
Residue number B
205
Peptide name
C-type lectin domain family 4 member E

Ligandability

Cysteine 108 of C-type lectin domain family 4 member E

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 205 of C-type lectin domain family 4 member E

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 C-type lectin domain family 4 member E between cysteines 179 and 197.

Details

Redox score ?
82
PDB code
3wh3
Structure name
human mincle, ligand free form
Structure deposition date
2013-08-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9ULY5
Residue number A
179
Residue number B
197
Peptide name
C-type lectin domain family 4 member E

Ligandability

Cysteine 179 of C-type lectin domain family 4 member E

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 197 of C-type lectin domain family 4 member E

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 C-type lectin domain family 4 member E between cysteines 79 and 80.

Details

Redox score ?
68
PDB code
3wh2
Structure name
human mincle in complex with citrate
Structure deposition date
2013-08-21
Thiol separation (Å)
6
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9ULY5
Residue number A
79
Residue number B
80
Peptide name
C-type lectin domain family 4 member E

Ligandability

Cysteine 79 of C-type lectin domain family 4 member E

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 80 of C-type lectin domain family 4 member E

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 C-type lectin domain family 4 member E between cysteines 79 and 91. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
58
PDB code
3wh3
Structure name
human mincle, ligand free form
Structure deposition date
2013-08-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9ULY5
Residue number A
79
Residue number B
91
Peptide name
C-type lectin domain family 4 member E

Ligandability

Cysteine 79 of C-type lectin domain family 4 member E

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 91 of C-type lectin domain family 4 member E

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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