7jqy

X-ray diffraction
2.15Å resolution

Crystal structure of Cfl1-D123S from Burkholderia cenocepacia

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
PDBe Complex ID:
PDB-CPX-110051 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 309 amino acids
Theoretical weight: 34.51 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli
UniProt:
  • Canonical: B4EJL9 (Residues: 1-309; Coverage: 100%)
Gene name: BCAM1529
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-1
Spacegroup: C2
Unit cell:
a: 195Å b: 98.4Å c: 170Å
α: 90° β: 118.6° γ: 90°
R-values:
R R work R free
0.21 0.209 0.24
Expression system: Escherichia coli