› 1uva

X-ray diffraction
2.5Å resolution

Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa

Released:
DOI: 10.2210/pdb1uva/pdb
PDB entry 1uva coloured by chain, front view.
PDB entry 1uva coloured by chain, side view.
PDB entry 1uva coloured by chain, top view.
Source organism: Oryza sativa
Primary publication:
Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa.
Cheng HC, Cheng PT, Peng P, Lyu PC, Sun YJ
Protein Sci 13 2304-15 (2004)
PMID: 15295114

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170968 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Non-specific lipid-transfer protein 1 Chain: A
Molecule details ›
Chain: A
Length: 91 amino acids
Theoretical weight: 8.92 KDa
Source organism: Oryza sativa
UniProt:
  • Canonical: Q0IQK9 (Residues: 26-116; Coverage: 100%)
Gene names: LOC_Os12g02320, LTP, Os12g0115100, OsJ_033644
Sequence domains: Protease inhibitor/seed storage/LTP family
Structure domains: Plant lipid-transfer and hydrophobic proteins

Ligands and Environments

1 bound ligand:
Ligand MYR 1 x MYR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 49.65Å b: 74.49Å c: 49.73Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.288

Quick links

Citations

8 review citations

Antimicrobial Peptides from Plants.
Tam et al. (2015)
7 more

5 mentions without citation

The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs).
Yeats et al. (2008)
4 more