C-type lectin domain family 2 member D

Intermolecular

Intramolecular

A redox-regulated disulphide may form between two units of C-type lectin domain family 2 member D at cysteines 75 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

4qkh

Structure name

dimeric form of human llt1, a ligand for nkr-p1

Structure deposition date

2014-06-06

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

C-type lectin domain family 2 member D

Peptide B name

C-type lectin domain family 2 member D

Peptide A accession

Q9UHP7

Peptide B accession

Q9UHP7

Peptide A residue number

Peptide B residue number

Ligandability

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 between two units of C-type lectin domain family 2 member D at cysteines 86 and 75. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?

PDB code

5mgt

Structure name

complex of human nkr-p1 and llt1 in deglycosylated forms

Structure deposition date

2016-11-22

Thiol separation (Å)

Half-sphere exposure sum ?

Minimum pK_a ?

nan

% buried

nan

Peptide A name

C-type lectin domain family 2 member D

Peptide B name

C-type lectin domain family 2 member D

Peptide A accession

Q9UHP7

Peptide B accession

Q9UHP7

Peptide A residue number

Peptide B residue number

Ligandability

Cysteine 86 of C-type lectin domain family 2 member D

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 75 of C-type lectin domain family 2 member D

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 2 member D between cysteines 163 and 63 (163 and 176 respectively in this structure).