› 1lgb

X-ray diffraction
3.3Å resolution

INTERACTION OF A LEGUME LECTIN WITH THE N2 FRAGMENT OF HUMAN LACTOTRANSFERRIN OR WITH THE ISOLATED BIANTENNARY GLYCOPEPTIDE: ROLE OF THE FUCOSE MOIETY

Released:
DOI: 10.2210/pdb1lgb/pdb
PDB entry 1lgb coloured by chain, front view.
PDB entry 1lgb coloured by chain, side view.
PDB entry 1lgb coloured by chain, top view.
Source organisms:
Primary publication:
Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.
Bourne Y, Mazurier J, Legrand D, Rougé P, Montreuil J, Spik G, Cambillau C
Structure 2 209-19 (1994)
PMID: 8069634

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero hexamer
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-136229 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Lectin beta-1 and beta-2 chains Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 19.8 KDa
Source organism: Lathyrus ochrus
UniProt:
  • Canonical: P04122 (Residues: 1-181; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls
Mannose/glucose-specific lectin alpha 2 chain Chain: B
Molecule details ›
Chain: B
Length: 53 amino acids
Theoretical weight: 5.92 KDa
Source organism: Lathyrus ochrus
UniProt:
  • Canonical: P12307 (Residues: 1-53; Coverage: 100%)
Sequence domains: Legume lectin domain
Lactotransferrin Chain: C
Molecule details ›
Chain: C
Length: 159 amino acids
Theoretical weight: 17.54 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02788 (Residues: 110-268; Coverage: 23%)
Gene names: GIG12, LF, LTF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GAL, FUC
Carbohydrate polymer
2 bound ligands:
Ligand MN 1 x MN
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 63.5Å b: 63.5Å c: 251.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 not available

Quick links

Citations

9 review citations

The structural role of sugars in glycoproteins.
Wyss et al. (1996)
8 more

4 mentions without citation

Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.
Goettig P. (2016)
3 more