ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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C-type lectin domain family 1 member B

Intramolecular
Cysteine 102 and cysteine 113
Cysteine 195 and cysteine 208
Cysteine 130 and cysteine 216
A redox-regulated disulphide may form within C-type lectin domain family 1 member B between cysteines 102 and 113.

Details

Redox score ?
86
PDB code
2c6u
Structure name
crystal structure of human clec-2 (clec1b)
Structure deposition date
2005-11-11
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P126
Residue number A
102
Residue number B
113
Peptide name
C-type lectin domain family 1 member B

Ligandability

Cysteine 102 of C-type lectin domain family 1 member B

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 113 of C-type lectin domain family 1 member B

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 1 member B between cysteines 195 and 208.

Details

Redox score ?
83
PDB code
3wwk
Structure name
crystal structure of clec-2 in complex with rhodocytin
Structure deposition date
2014-06-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
73
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P126
Residue number A
195
Residue number B
208
Peptide name
C-type lectin domain family 1 member B

Ligandability

Cysteine 195 of C-type lectin domain family 1 member B

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 208 of C-type lectin domain family 1 member B

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 1 member B between cysteines 130 and 216.

Details

Redox score ?
82
PDB code
3wwk
Structure name
crystal structure of clec-2 in complex with rhodocytin
Structure deposition date
2014-06-20
Thiol separation (Å)
2
Half-sphere exposure sum ?
69
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9P126
Residue number A
130
Residue number B
216
Peptide name
C-type lectin domain family 1 member B

Ligandability

Cysteine 130 of C-type lectin domain family 1 member B

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 216 of C-type lectin domain family 1 member B

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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