2fc3

X-ray diffraction
1.56Å resolution

Crystal structure of the extremely thermostable Aeropyrum pernix L7Ae multifunctional protein

Released:
Source organism: Aeropyrum pernix
Primary publication:
Structure of the Aeropyrum pernix L7Ae multifunctional protein and insight into its extreme thermostability.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69 979-88 (2013)
PMID: 23989144

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
50S ribosomal protein L7Ae Chain: A
Molecule details ›
Chain: A
Length: 124 amino acids
Theoretical weight: 13.63 KDa
Source organism: Aeropyrum pernix
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YAX7 (Residues: 4-127; Coverage: 98%)
Gene names: APE_1818, rpl7ae
Sequence domains: Ribosomal protein L7Ae/L30e/S12e/Gadd45 family
Structure domains: 60s Ribosomal Protein L30; Chain: A;

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 35.054Å b: 49.188Å c: 65.048Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.226
Expression system: Escherichia coli