› 1xd5

X-ray diffraction
2Å resolution

Crystal structures of novel monomeric monocot mannose-binding lectins from Gastrodia elata

Released:
DOI: 10.2210/pdb1xd5/pdb
PDB entry 1xd5 coloured by chain, front view.
PDB entry 1xd5 coloured by chain, side view.
PDB entry 1xd5 coloured by chain, top view.
Source organism: Gastrodia elata
Primary publication:
Structural mechanism governing the quaternary organization of monocot mannose-binding lectin revealed by the novel monomeric structure of an orchid lectin.
Liu W, Yang N, Ding J, Huang RH, Hu Z, Wang DC
J Biol Chem 280 14865-76 (2005)
PMID: 15649901

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-189611 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bulb-type lectin domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 112 amino acids
Theoretical weight: 12.31 KDa
Source organism: Gastrodia elata
UniProt:
  • Canonical: Q9AXZ2 (Residues: 29-140; Coverage: 72%)
Structure domains: Bulb-type lectin domain

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P21212
Unit cell:
a: 61.087Å b: 91.488Å c: 81.132Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.165 0.206

Quick links

Citations

2 review citations

Inhibition of HIV entry by carbohydrate-binding proteins.
Balzarini J. (2006)
1 more

3 mentions without citation

β-Propeller blades as ancestral peptides in protein evolution.
Kopec et al. (2013)
2 more