› 4ao9

X-ray diffraction
1.5Å resolution

Biochemical properties and crystal structure of a novel beta- phenylalanine aminotransferase from Variovorax paradoxus

Released:
DOI: 10.2210/pdb4ao9/pdb
PDB 4ao9 coloured by chain and viewed from the front.
PDB 4ao9 coloured by chain and viewed from the side.
PDB 4ao9 coloured by chain and viewed from the top.
Source organism: Variovorax paradoxus
Primary publication:
Biochemical properties and crystal structure of a ��-phenylalanine aminotransferase from Variovorax paradoxus.
Crismaru CG, Wybenga GG, Szymanski W, Wijma HJ, Wu B, Bartsch S, de Wildeman S, Poelarends GJ, Feringa BL, Dijkstra BW, Janssen DB
Appl. Environ. Microbiol. (2012)
PMID: 23087034

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-phenylalanine transaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 454 amino acids
Theoretical weight: 48.63 KDa
Source organism: Variovorax paradoxus
Expression system: Escherichia coli
UniProt:
  • Canonical: H8WR05 (Residues: 1-434; Coverage: 100%)
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PLP 2 x PLP
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 88.74Å b: 100.11Å c: 104.799Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.182
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Enzymatic asymmetric synthesis of chiral amino acids.
Xue et al. (2018)
2 more

1 mention without citation

Biochemical properties and crystal structure of a β-phenylalanine aminotransferase from Variovorax paradoxus.
Crismaru et al. (2013)