› 3tr2

X-ray diffraction
2Å resolution

Structure of a orotidine 5'-phosphate decarboxylase (pyrF) from Coxiella burnetii

Released:
DOI: 10.2210/pdb3tr2/pdb
PDB entry 3tr2 coloured by chain, front view.
PDB entry 3tr2 coloured by chain, side view.
PDB entry 3tr2 coloured by chain, top view.
Source organism: Coxiella burnetii
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

Function and Biology Details

Reaction catalysed: 
Orotidine 5'-phosphate = UMP + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182935 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Orotidine 5'-phosphate decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 239 amino acids
Theoretical weight: 26.53 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83E06 (Residues: 1-236; Coverage: 100%)
Gene names: CBU_0531, pyrF
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 40.62Å b: 99.676Å c: 110.565Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.217
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
4 more