1c7g

X-ray diffraction
2.1Å resolution

TYROSINE PHENOL-LYASE FROM ERWINIA HERBICOLA

Released:
Entry authors: Mikami B, Yamamoto Y, Katayama T, Suzuki H

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine phenol-lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 456 amino acids
Theoretical weight: 51.43 KDa
Source organism: Pantoea agglomerans pv. gypsophilae
Expression system: Escherichia coli
UniProt:
  • Canonical: P31011 (Residues: 1-456; Coverage: 100%)
Gene names: tpl, tutA
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE M18X
Spacegroup: P21212
Unit cell:
a: 163.49Å b: 113.04Å c: 101.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 0.242
Expression system: Escherichia coli