1bwu

X-ray diffraction
2.8Å resolution

MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM GARLIC (ALLIUM SATIVUM) BULBS COMPLEXED WITH ALPHA-D-MANNOSE

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer (preferred)
hetero dimer
PDBe Complex ID:
PDB-CPX-174360 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Bulb-type lectin domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.87 KDa
Source organism: Allium sativum
UniProt:
  • Canonical: Q38789 (Residues: 177-282; Coverage: 38%)
Gene name: LECASAI3
Structure domains: Bulb-type lectin domain
Bulb-type lectin domain-containing protein Chain: D
Molecule details ›
Chain: D
Length: 109 amino acids
Theoretical weight: 12.12 KDa
Source organism: Allium sativum
UniProt:
  • Canonical: Q38784 (Residues: 18-126; Coverage: 86%)
Gene name: ASAII2
Structure domains: Bulb-type lectin domain
Bulb-type lectin domain-containing protein Chain: P
Molecule details ›
Chain: P
Length: 106 amino acids
Theoretical weight: 11.68 KDa
Source organism: Allium sativum
UniProt:
  • Canonical: Q38789 (Residues: 177-282; Coverage: 38%)
Gene name: LECASAI3
Structure domains: Bulb-type lectin domain
Bulb-type lectin domain-containing protein Chain: Q
Molecule details ›
Chain: Q
Length: 109 amino acids
Theoretical weight: 12.01 KDa
Source organism: Allium sativum
UniProt:
  • Canonical: Q38784 (Residues: 18-126; Coverage: 86%)
Gene name: ASAII2
Structure domains: Bulb-type lectin domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 203.243Å b: 43.78Å c: 79.268Å
α: 90° β: 112.37° γ: 90°
R-values:
R R work R free
0.226 0.226 0.278