C-type lectin domain family 4, member b1

Intramolecular

A redox-regulated disulphide may form within C-type lectin domain family 4, member b1 between cysteines 45 and 56 (78 and 89 respectively in this structure).

Details

Redox score ?

PDB code

6lkr

Structure name

crystal structure of mouse dcar2 crd domain complex

Structure deposition date

2019-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Q9D8Q7

Residue number A

Residue number B

Peptide name

C-type lectin domain family 4, member b1

Ligandability

Cysteine 45 of C-type lectin domain family 4, member b1

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 56 of C-type lectin domain family 4, member b1

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 b1 between cysteines 143 and 161 (176 and 194 respectively in this structure).

Details

Redox score ?

PDB code

6lkr

Structure name

crystal structure of mouse dcar2 crd domain complex

Structure deposition date

2019-12-20

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide accession

Q9D8Q7

Residue number A

143

Residue number B

161

Peptide name

C-type lectin domain family 4, member b1

Ligandability

Cysteine 143 of C-type lectin domain family 4, member b1

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 161 of C-type lectin domain family 4, member b1

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 b1 between cysteines 75 and 169 (108 and 202 respectively in this structure).