3wxm

X-ray diffraction
2.3Å resolution

Crystal structure of archaeal Pelota and GTP-bound EF1 alpha complex

Released:
Source organism: Aeropyrum pernix K1

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Elongation factor 1-alpha Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 447 amino acids
Theoretical weight: 49.66 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9YAV0 (Residues: 1-437; Coverage: 100%)
Gene names: APE_1844, tuf
Sequence domains:
Structure domains:
Protein pelota homolog Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 376 amino acids
Theoretical weight: 41.47 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9YAZ5 (Residues: 1-356; Coverage: 100%)
Gene names: APE_1800.1, pelA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2221
Unit cell:
a: 148.926Å b: 158.944Å c: 427.236Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.198 0.261
Expression system: Escherichia coli BL21(DE3)