› 1loe

X-ray diffraction
1.9Å resolution

X-RAY CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT AT 1.9 ANGSTROMS RESOLUTION OF ISOLECTIN I FROM THE SEEDS OF LATHYRUS OCHRUS

Released:
DOI: 10.2210/pdb1loe/pdb
PDB entry 1loe coloured by chain, front view.
PDB entry 1loe coloured by chain, side view.
PDB entry 1loe coloured by chain, top view.
Source organism: Lathyrus ochrus
Primary publication:
X-ray crystal structure determination and refinement at 1.9 A resolution of isolectin I from the seeds of Lathyrus ochrus.
Bourne Y, Abergel C, Cambillau C, Frey M, Rougé P, Fontecilla-Camps JC
J Mol Biol 214 571-84 (1990)
PMID: 2380988

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137409 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lectin beta-1 and beta-2 chains Chains: A, C
Molecule details ›
Chains: A, C
Length: 181 amino acids
Theoretical weight: 19.85 KDa
Source organism: Lathyrus ochrus
Expression system: Not provided
UniProt:
  • Canonical: P04122 (Residues: 1-181; Coverage: 100%)
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls
Mannose/glucose-specific lectin alpha 1 chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 52 amino acids
Theoretical weight: 5.78 KDa
Source organism: Lathyrus ochrus
Expression system: Not provided
UniProt:
  • Canonical: P12306 (Residues: 1-52; Coverage: 98%)
Sequence domains: Legume lectin domain

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 135.84Å b: 63.12Å c: 54.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 not available
Expression system: Not provided

Quick links

Citations

4 review citations

Mannose-binding plant lectins: different structural scaffolds for a common sugar-recognition process.
Barre et al. (2001)
3 more

1 mention without citation

Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.
Barre et al. (2019)