3vz6

X-ray diffraction
1.5Å resolution

Crystal Structure Analysis of the Mini-chaperonines, variant with Gly 184 replaced with Ile and Leu 185 replaced Val and Val 186 replaced with Leu.

Released:
Source organism: Escherichia coli K-12
Entry authors: Saijo S, Sato T

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin GroEL Chain: A
Molecule details ›
Chain: A
Length: 199 amino acids
Theoretical weight: 21.6 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 190-376; Coverage: 34%)
Gene names: JW4103, b4143, groEL, groL, mopA
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains: GroEL

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21212
Unit cell:
a: 75.492Å b: 79.9Å c: 35.192Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.268 0.268 0.288
Expression system: Escherichia coli