› 1asx

X-ray diffraction
2.8Å resolution

APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM

Released:
DOI: 10.2210/pdb1asx/pdb
PDB entry 1asx coloured by chain, front view.
PDB entry 1asx coloured by chain, side view.
PDB entry 1asx coloured by chain, top view.
Source organism: Thermoplasma acidophilum
Primary publication:
Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin.
Klumpp M, Baumeister W, Essen LO
Cell 91 263-70 (1997)
PMID: 9346243

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155723 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermosome subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.82 KDa
Source organism: Thermoplasma acidophilum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P48424 (Residues: 213-365; Coverage: 28%)
Gene names: Ta0980, thsA
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains: GroEL

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P3121
Unit cell:
a: 79.91Å b: 79.91Å c: 70.25Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.222 0.272
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

29 review citations

The Hsp70 and Hsp60 chaperone machines.
Bukau et al. (1998)
28 more