3upy

X-ray diffraction
1.8Å resolution

Crystal structure of the Brucella abortus enzyme catalyzing the first committed step of the methylerythritol 4-phosphate pathway.

Released:
Model geometry
Fit model/data

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-174150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SAF domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 445 amino acids
Theoretical weight: 47.66 KDa
Source organism: Brucella abortus 2308
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2YIM3 (Residues: 1-437; Coverage: 100%)
Gene name: BAB2_0264
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P1
Unit cell:
a: 49.391Å b: 63.379Å c: 79.334Å
α: 68.79° β: 75.54° γ: 72.07°
R-values:
R R work R free
0.165 0.163 0.204
Expression system: Escherichia coli