1ybz

X-ray diffraction
1.82Å resolution

Conserved hypothetical protein from Pyrococcus furiosus Pfu-1581948-001

Released:
Source organism: Pyrococcus furiosus
Entry authors: Lee D, Chen L, Nguyen D, Dillard BD, Tempel W, Habel J, Zhou W, Chang S-H, Kelley L-LC, Liu Z-J, Lin D, Zhang H, Praissman J, Bridger S, Eneh JC, Hopkins RC, Jenney Jr FE, Lee H-S, Li T, Poole II FL, Shah C, Sugar FJ, Adams MWW, Rose JP, Wang B-C, Southeast Collaboratory for Structural Genomics (SECSG)

Function and Biology Details

Reaction catalysed:
Chorismate = prephenate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-186376 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chorismate mutase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 91 amino acids
Theoretical weight: 10.87 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8U098 (Residues: 2-76; Coverage: 99%)
Gene name: PF1701
Sequence domains: Chorismate mutase type II
Structure domains: Chorismate mutase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P43212
Unit cell:
a: 52.501Å b: 52.501Å c: 80.217Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.201 0.237
Expression system: Escherichia coli