› 4jm3

X-ray diffraction
1.85Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179133 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enduracididine biosynthesis enzyme MppR Chains: A, B
Molecule details ›
Chains: A, B
Length: 302 amino acids
Theoretical weight: 32.26 KDa
Source organism: Streptomyces hygroscopicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q643B8 (Residues: 1-302; Coverage: 100%)
Gene name: mppR
Sequence domains: Acetoacetate decarboxylase (ADC)
Structure domains: Acetoacetate decarboxylase-like

Ligands and Environments

1 bound ligand:
Ligand EPE 2 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P3121
Unit cell:
a: 109.79Å b: 109.79Å c: 87.69Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.146 0.145 0.176
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Nonribosomal Peptide Synthesis-Principles and Prospects.
Süssmuth et al. (2017)
6 more

3 mentions without citation

Structural and functional characterization of MppR, an enduracididine biosynthetic enzyme from streptomyces hygroscopicus: functional diversity in the acetoacetate decarboxylase-like superfamily.
Burroughs et al. (2013)
2 more