PDBe 1efx

X-ray diffraction
3Å resolution

STRUCTURE OF A COMPLEX BETWEEN THE HUMAN NATURAL KILLER CELL RECEPTOR KIR2DL2 AND A CLASS I MHC LIGAND HLA-CW3

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
HLA class I histocompatibility antigen, Cw-3 alpha chain Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 32.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04222 (Residues: 25-302; Coverage: 81%)
Gene names: HLA-C, HLAC
Sequence domains:
Structure domains:
Beta-2-microglobulin Chain: B
Molecule details ›
Chain: B
Length: 100 amino acids
Theoretical weight: 11.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61769 (Residues: 21-119; Coverage: 100%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Importin subunit alpha-1 Chain: C
Molecule details ›
Chain: C
Length: 9 amino acids
Theoretical weight: 868 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P52292 (Residues: 204-212; Coverage: 2%)
Gene names: KPNA2, RCH1, SRP1
Killer cell immunoglobulin-like receptor 2DL2 Chains: D, E
Molecule details ›
Chains: D, E
Length: 200 amino acids
Theoretical weight: 22.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P43627 (Residues: 22-221; Coverage: 61%)
Gene names: CD158B1, KIR2DL2, NKAT6
Sequence domains: Immunoglobulin domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P212121
Unit cell:
a: 68.54Å b: 90.33Å c: 207.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.231 0.294
Expression systems:
  • Escherichia coli
  • Not provided