ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-type lectin domain family 7 member A

Intramolecular
Cysteine 119 and cysteine 130
Cysteine 219 and cysteine 232
Cysteine 147 and cysteine 240
A redox-regulated disulphide may form within C-type lectin domain family 7 member A between cysteines 119 and 130.

Details

Redox score ?
83
PDB code
2bph
Structure name
structure of murine dectin-1
Structure deposition date
2005-04-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
66
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6QLQ4
Residue number A
119
Residue number B
130
Peptide name
C-type lectin domain family 7 member A

Ligandability

Cysteine 119 of C-type lectin domain family 7 member A

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 130 of C-type lectin domain family 7 member A

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 7 member A between cysteines 219 and 232.

Details

Redox score ?
81
PDB code
2cl8
Structure name
dectin-1 in complex with beta-glucan
Structure deposition date
2006-04-26
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6QLQ4
Residue number A
219
Residue number B
232
Peptide name
C-type lectin domain family 7 member A

Ligandability

Cysteine 219 of C-type lectin domain family 7 member A

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 232 of C-type lectin domain family 7 member A

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 7 member A between cysteines 147 and 240.

Details

Redox score ?
80
PDB code
2bpe
Structure name
structure of murine dectin-1
Structure deposition date
2005-04-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
75
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6QLQ4
Residue number A
147
Residue number B
240
Peptide name
C-type lectin domain family 7 member A

Ligandability

Cysteine 147 of C-type lectin domain family 7 member A

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 240 of C-type lectin domain family 7 member A

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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