ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-type lectin domain family 9 member A

Intramolecular
Cysteine 113 and cysteine 124
Cysteine 211 and cysteine 224
Cysteine 141 and cysteine 232
A redox-regulated disulphide may form within C-type lectin domain family 9 member A between cysteines 113 and 124.

Details

Redox score ?
85
PDB code
3vpp
Structure name
crystal structure of the human clec9a c-type lectin-like domain
Structure deposition date
2012-03-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6UXN8
Residue number A
113
Residue number B
124
Peptide name
C-type lectin domain family 9 member A

Ligandability

Cysteine 113 of C-type lectin domain family 9 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 124 of C-type lectin domain family 9 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 9 member A between cysteines 211 and 224.

Details

Redox score ?
85
PDB code
3vpp
Structure name
crystal structure of the human clec9a c-type lectin-like domain
Structure deposition date
2012-03-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6UXN8
Residue number A
211
Residue number B
224
Peptide name
C-type lectin domain family 9 member A

Ligandability

Cysteine 211 of C-type lectin domain family 9 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 224 of C-type lectin domain family 9 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 9 member A between cysteines 141 and 232.

Details

Redox score ?
82
PDB code
3vpp
Structure name
crystal structure of the human clec9a c-type lectin-like domain
Structure deposition date
2012-03-07
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q6UXN8
Residue number A
141
Residue number B
232
Peptide name
C-type lectin domain family 9 member A

Ligandability

Cysteine 141 of C-type lectin domain family 9 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 9 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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