› 5hy1

X-ray diffraction
2.01Å resolution

high resolution structure of barbiturase

Released:
DOI: 10.2210/pdb5hy1/pdb
PDB entry 5hy1 coloured by chain, front view.
PDB entry 5hy1 coloured by chain, side view.
PDB entry 5hy1 coloured by chain, top view.
Source organism: Rhodococcus erythropolis
Primary publication:
High-Resolution X-Ray Structures of Two Functionally Distinct Members of the Cyclic Amide Hydrolase Family of Toblerone Fold Enzymes.
Peat TS, Balotra S, Wilding M, Hartley CJ, Newman J, Scott C
Appl Environ Microbiol 83 (2017)
PMID: 28235873

Function and Biology Details

Reaction catalysed: 
Barbiturate + H(2)O = 3-oxo-3-ureidopropanoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186034 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Barbiturase Chain: A
Molecule details ›
Chain: A
Length: 389 amino acids
Theoretical weight: 41.19 KDa
Source organism: Rhodococcus erythropolis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8RSQ2 (Residues: 1-369; Coverage: 100%)
Gene name: bar
Sequence domains: Amidohydrolase ring-opening protein (Amido_AtzD_TrzD)
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand WDL 1 x WDL
Ligand NA 1 x NA
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: I222
Unit cell:
a: 69.403Å b: 82.356Å c: 114.552Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.223
Expression system: Escherichia coli BL21

Quick links

Citations

3 citation in other articles

An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.
Esquirol et al. (2018)
2 more

1 mention without citation

High-Resolution X-Ray Structures of Two Functionally Distinct Members of the Cyclic Amide Hydrolase Family of Toblerone Fold Enzymes.
Peat et al. (2017)