7xoq

Electron Microscopy
3.3Å resolution

Cryo-EM structure of occupied ring subunit 2 (OR2) of GroEL from GroEL-UGT1A double occupied ring complex

Released:
Source organism: Escherichia coli
Entry authors: Stapleton K, Takagi J, Mizohata E
Related structures: EMD-33356

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide

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: K
Molecule details ›
Chain: K
Length: 547 amino acids
Theoretical weight: 57.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6F5 (Residues: 2-548; Coverage: 100%)
Gene names: JW4103, b4143, groEL, groL, mopA
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-33356
Expression system: Escherichia coli