4f0j

X-ray diffraction
1.5Å resolution

Crystal structure of a probable hydrolytic enzyme (PA3053) from Pseudomonas aeruginosa PAO1 at 1.50 A resolution

Released:
Source organism: Pseudomonas aeruginosa PAO1
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-191191 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 35.87 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HZF5 (Residues: 22-335; Coverage: 100%)
Gene name: PA3053
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P21212
Unit cell:
a: 63.234Å b: 82.886Å c: 58.464Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.186
Expression system: Escherichia coli