› 4l39

X-ray diffraction
2.81Å resolution

Crystal structure of GH3.12 from Arabidopsis thaliana in complex with AMPCPP and salicylate

Released:
DOI: 10.2210/pdb4l39/pdb
PDB entry 4l39 coloured by chain, front view.
PDB entry 4l39 coloured by chain, side view.
PDB entry 4l39 coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Determination of the GH3.12 protein conformation through HPLC-integrated SAXS measurements combined with X-ray crystallography.
Round A, Brown E, Marcellin R, Kapp U, Westfall CS, Jez JM, Zubieta C
Acta Crystallogr D Biol Crystallogr 69 2072-80 (2013)
PMID: 24100325

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192345 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-substituted benzoates-glutamate ligase GH3.12 Chains: A, B
Molecule details ›
Chains: A, B
Length: 581 amino acids
Theoretical weight: 65.76 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9LYU4 (Residues: 1-575; Coverage: 100%)
Gene names: At5g13320, GDG1, GH3.12, PBS3, T22N19.5, T31B5.140, WIN3
Sequence domains: GH3 auxin-responsive promoter

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand SAL 2 x SAL
Ligand APC 2 x APC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 62.36Å b: 114.088Å c: 157.976Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.267
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Weak protein-ligand interactions studied by small-angle X-ray scattering.
Tuukkanen et al. (2014)
1 more

1 mention without citation

Analysis and validation of macromolecular B values.
Masmaliyeva et al. (2019)