› 4qkj

X-ray diffraction
2.75Å resolution

Glycosylated form of human LLT1, a ligand for NKR-P1, in this structure forming hexamers

Released:
DOI: 10.2210/pdb4qkj/pdb
PDB entry 4qkj coloured by chain, front view.
PDB entry 4qkj coloured by chain, side view.
PDB entry 4qkj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.
Skálová T, Bláha J, Harlos K, Dušková J, Koval' T, Stránský J, Hašek J, Vaněk O, Dohnálek J
Acta Crystallogr D Biol Crystallogr 71 578-91 (2015)
PMID: 25760607

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193760 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C-type lectin domain family 2 member D Chain: A
Molecule details ›
Chain: A
Length: 135 amino acids
Theoretical weight: 15.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q9UHP7 (Residues: 72-191; Coverage: 63%)
Gene names: CLAX, CLEC2D, LLT1, OCIL
Sequence domains: Lectin C-type domain
Structure domains: Mannose-Binding Protein A, subunit A

Ligands and Environments

1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6322
Unit cell:
a: 70.06Å b: 70.06Å c: 101.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.221 0.298
Expression system: Homo sapiens

Quick links

Citations

2 review citations

LLT1-CD161 Interaction in Cancer: Promises and Challenges.
Braud et al. (2022)
1 more

1 mention without citation

Four crystal structures of human LLT1, a ligand of human NKR-P1, in varied glycosylation and oligomerization states.
Skálová et al. (2015)