› 1bqp

X-ray diffraction
2.1Å resolution

THE STRUCTURE OF THE PEA LECTIN-D-MANNOPYRANOSE COMPLEX

Released:
DOI: 10.2210/pdb1bqp/pdb
PDB entry 1bqp coloured by chain, front view.
PDB entry 1bqp coloured by chain, side view.
PDB entry 1bqp coloured by chain, top view.
Source organism: Pisum sativum
Primary publication:
The Structure of the Pea Lectin-D-Mannopyranose Complex at a 2.1 A Resolution
Ruzheinikov SN, Mikhailova IY, Tsygannik IN, Pangborn W, Duax W, Pletnev VZ
Russ. J. Bioorganic Chem. 24 277-279 (1998)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-136275 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lectin beta chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 181 amino acids
Theoretical weight: 20 KDa
Source organism: Pisum sativum
UniProt:
  • Canonical: P02867 (Residues: 31-211; Coverage: 74%)
Gene names: LECA, PSL1
Sequence domains: Legume lectin domain
Structure domains: Jelly Rolls
Lectin alpha chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 47 amino acids
Theoretical weight: 5.18 KDa
Source organism: Pisum sativum
UniProt:
  • Canonical: P02867 (Residues: 218-264; Coverage: 19%)
Gene names: LECA, PSL1

Ligands and Environments

4 bound ligands:
Ligand CA 2 x CA
Ligand MN 2 x MN
Ligand MAN 2 x MAN
Ligand BMA 2 x BMA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 73.926Å b: 104.083Å c: 64.837Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 0.188

Quick links

Citations

1 mention without citation

NMR and Molecular Recognition of N-Glycans: Remote Modifications of the Saccharide Chain Modulate Binding Features.
Gimeno et al. (2017)