› 4dol

X-ray diffraction
1.7Å resolution

Crystal structure of Arabidopsis thaliana fatty-acid binding protein At1g53520 (AtFAP3)

Released:
DOI: 10.2210/pdb4dol/pdb
PDB entry 4dol coloured by chain, front view.
PDB entry 4dol coloured by chain, side view.
PDB entry 4dol coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis.
Ngaki MN, Louie GV, Philippe RN, Manning G, Pojer F, Bowman ME, Li L, Larsen E, Wurtele ES, Noel JP
Nature 485 530-3 (2012)
PMID: 22622584

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189930 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty-acid-binding protein 3, chloroplastic Chain: A
Molecule details ›
Chain: A
Length: 217 amino acids
Theoretical weight: 23.13 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9C8L2 (Residues: 71-287; Coverage: 76%)
Gene names: At1g53520, F22G10.11, FAP3, T3F20.16
Sequence domains: Chalcone-flavanone isomerase
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 51.908Å b: 52.911Å c: 95.563Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

The flavonoid biosynthetic pathway in Arabidopsis: structural and genetic diversity.
Saito et al. (2013)
24 more

5 mentions without citation

Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis.
Ngaki et al. (2012)
4 more