6s7j

X-ray diffraction
2.2Å resolution

Native crystal structure of ergothioneine degrading enzyme Ergothionase from Treponema denticola

Released:
Source organism: Treponema denticola SP33
Primary publication:
Structure and Mechanism of Ergothionase from Treponema denticola.
Chemistry 25 10298-10303 (2019)
PMID: 31188501

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-125972 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine and histidine ammonia-lyase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 497 amino acids
Theoretical weight: 55.7 KDa
Source organism: Treponema denticola SP33
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: M2BPW8 (Residues: 2-498; Coverage: 100%)
Gene name: HMPREF9733_00339
Sequence domains: Aromatic amino acid lyase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P1
Unit cell:
a: 76.906Å b: 76.956Å c: 177.567Å
α: 78.09° β: 82.02° γ: 79.78°
R-values:
R R work R free
0.219 0.217 0.267
Expression system: Escherichia coli BL21(DE3)