› 5wjp

X-ray diffraction
1.57Å resolution

Crystal structure of the cyclohexadienyl dehydratase-like solute-binding protein SAR11_1068 from Candidatus Pelagibacter ubique.

Released:
DOI: 10.2210/pdb5wjp/pdb
PDB entry 5wjp coloured by chain, front view.
PDB entry 5wjp coloured by chain, side view.
PDB entry 5wjp coloured by chain, top view.
Source organism: Candidatus Pelagibacter ubique HTCC1062
Primary publication:
Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein.
Clifton BE, Kaczmarski JA, Carr PD, Gerth ML, Tokuriki N, Jackson CJ
Nat Chem Biol 14 542-547 (2018)
PMID: 29686357

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175508 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Solute-binding protein family 3/N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 27.9 KDa
Source organism: Candidatus Pelagibacter ubique HTCC1062
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4FLR5 (Residues: 19-255; Coverage: 100%)
Gene names: SAR11_1068, pheC
Sequence domains: Bacterial extracellular solute-binding proteins, family 3
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 38.73Å b: 65.87Å c: 90.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Conformational dynamics and enzyme evolution.
Petrović et al. (2018)
9 more