› 2plh

X-ray diffraction
2.5Å resolution

STRUCTURE OF ALPHA-1-PUROTHIONIN AT ROOM TEMPERATURE AND 2.8 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb2plh/pdb
PDB entry 2plh coloured by chain, front view.
PDB entry 2plh coloured by chain, side view.
PDB entry 2plh coloured by chain, top view.
Source organism: Triticum aestivum
Primary publication:
Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 1: alpha1-purothionin revisited.
Rao U, Stec B, Teeter MM
Acta Crystallogr D Biol Crystallogr 51 904-13 (1995)
PMID: 15299760

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-1-purothionin Chain: A
Molecule details ›
Chain: A
Length: 45 amino acids
Theoretical weight: 4.84 KDa
Source organism: Triticum aestivum
UniProt:
  • Canonical: P01544 (Residues: 17-61; Coverage: 41%)
Gene names: PUR-D1, THI1.1
Sequence domains: Plant thionin
Structure domains: Thionin-like

Ligands and Environments

4 bound ligands:
Ligand ACT 3 x ACT
Ligand PO4 1 x PO4
Ligand SBT 2 x SBT
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I422
Unit cell:
a: 53.59Å b: 53.59Å c: 69.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 not available not available

Quick links

Citations

6 review citations

Plant defense peptides.
García-Olmedo et al. (1998)
5 more

1 mention without citation

Characterization of protein secondary structure from NMR chemical shifts.
Mielke et al. (2009)