2pim

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF A PUTATIVE THIOESTERASE, PHENYLACETIC ACID DEGRADATION-RELATED PROTEIN (REUT_B4779) FROM RALSTONIA EUTROPHA JMP134 AT 2.20 A RESOLUTION

Released:
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
PDBe Complex ID:
PDB-CPX-175192 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl-CoA thioesterase-like N-terminal HotDog domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 15 KDa
Source organism: Cupriavidus pinatubonensis JMP134
Expression system: Escherichia coli
UniProt:
  • Canonical: Q46RV7 (Residues: 1-140; Coverage: 100%)
Gene name: Reut_B4779
Sequence domains: Acyl-CoA thioesterase N-terminal domain
Structure domains: Hotdog Thioesterase

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P622
Unit cell:
a: 111.774Å b: 111.774Å c: 46.461Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.182 0.222
Expression system: Escherichia coli