› 4fl0

X-ray diffraction
2.3Å resolution

Crystal structure of ALD1 from Arabidopsis thaliana

Released:
DOI: 10.2210/pdb4fl0/pdb
PDB entry 4fl0 coloured by chain, front view.
PDB entry 4fl0 coloured by chain, side view.
PDB entry 4fl0 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structure of ALD1, a plant-specific homologue of the universal diaminopimelate aminotransferase enzyme of lysine biosynthesis.
Sobolev V, Edelman M, Dym O, Unger T, Albeck S, Kirma M, Galili G
Acta Crystallogr Sect F Struct Biol Cryst Commun 69 84-9 (2013)
PMID: 23385743

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195700 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase ALD1, chloroplastic Chains: A, B
Molecule details ›
Chains: A, B
Length: 456 amino acids
Theoretical weight: 50.64 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZQI7 (Residues: 1-456; Coverage: 100%)
Gene names: ALD1, At2g13810, F13J11.16
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 57.28Å b: 89.87Å c: 180.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.241
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Biochemical Principles and Functional Aspects of Pipecolic Acid Biosynthesis in Plant Immunity.
Hartmann et al. (2017)
3 more

2 mentions without citation

ALD1 accumulation in Arabidopsis epidermal plastids confers local and non-autonomous disease resistance.
Jiang et al. (2021)
1 more