› 3gsh

X-ray diffraction
1.8Å resolution

Three-dimensional structure of a post translational modified barley LTP1

Released:
DOI: 10.2210/pdb3gsh/pdb
PDB entry 3gsh coloured by chain, front view.
PDB entry 3gsh coloured by chain, side view.
PDB entry 3gsh coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins.
Bakan B, Hamberg M, Larue V, Prangé T, Marion D, Lascombe MB
Biochem Biophys Res Commun 390 780-5 (2009)
PMID: 19836358

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139653 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Non-specific lipid-transfer protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 91 amino acids
Theoretical weight: 9.7 KDa
Source organism: Hordeum vulgare
UniProt:
  • Canonical: P07597 (Residues: 27-117; Coverage: 100%)
Gene names: LTP1, PAPI
Sequence domains: Protease inhibitor/seed storage/LTP family
Structure domains: Plant lipid-transfer and hydrophobic proteins

Ligands and Environments

4 bound ligands:
Ligand ZN 4 x ZN
Ligand NA 3 x NA
Ligand TFA 2 x TFA
Ligand ASY 2 x ASY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 28.74Å b: 76.133Å c: 39.402Å
α: 90° β: 104.34° γ: 90°
R-values:
R R work R free
0.203 0.194 0.262

Quick links

Citations

2 review citations

Peptide promiscuity: an evolutionary concept for plant defense.
Franco OL. (2011)
1 more

7 mentions without citation

Lipid transfer proteins: classification, nomenclature, structure, and function.
Salminen et al. (2016)
6 more