› 6h2o

X-ray diffraction
1.9Å resolution

APO structure of Phenylalanine ammonia-lyase from Petroselinum crispum

Released:
DOI: 10.2210/pdb6h2o/pdb
PDB entry 6h2o coloured by chain, front view.
PDB entry 6h2o coloured by chain, side view.
PDB entry 6h2o coloured by chain, top view.
Source organism: Petroselinum crispum
Primary publication:
Substrate Tunnel Engineering Aided by X-ray Crystallography and Functional Dynamics Swaps the Function of MIO-Enzymes
Bata Z, Molnar Z, Madaras E, Molnar B, Santa-Bell E, Varga A, Leveles I, Qian R, Hammerschmidt F, Paizs C, Vertessy BG, Poppe L
ACS Catalysis 4538-4549 (2021)

Function and Biology Details

Reaction catalysed: 
L-phenylalanine = trans-cinnamate + ammonia
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150239 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine ammonia-lyase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 714 amino acids
Theoretical weight: 77.85 KDa
Source organism: Petroselinum crispum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P24481 (Residues: 1-716; Coverage: 100%)
Gene name: PAL1
Sequence domains: Aromatic amino acid lyase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MDO 2 x MDO

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2221
Unit cell:
a: 119.89Å b: 161.12Å c: 141.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.206
Expression system: Escherichia coli BL21(DE3)

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