› 2yhk

X-ray diffraction
1.91Å resolution

D214A mutant of tyrosine phenol-lyase from Citrobacter freundii

Released:
DOI: 10.2210/pdb2yhk/pdb
PDB entry 2yhk coloured by chain, front view.
PDB entry 2yhk coloured by chain, side view.
PDB entry 2yhk coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Crystal Structure of Citrobacter Freundii Asp214Ala Tyrosine Phenol-Lyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine
Milic D, Demidkina TV, Zakomirdina LN, Matkovic-Calogovic D, Antson AA
Croatica Chemica Acta 85 283- (2012)

Function and Biology Details

Reaction catalysed: 
(1a) L-tyrosine = phenol + 2-aminoprop-2-enoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine phenol-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 456 amino acids
Theoretical weight: 51.52 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
  • Canonical: P31013 (Residues: 1-456; Coverage: 100%)
Gene name: tpl
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
4 bound ligands:
Ligand K 2 x K
Ligand PG4 1 x PG4
Ligand PEG 6 x PEG
Ligand P33 1 x P33
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21212
Unit cell:
a: 132.605Å b: 142.705Å c: 59.412Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.156 0.177
Expression system: Escherichia coli

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