3e76

X-ray diffraction
3.94Å resolution

Crystal structure of Wild-type GroEL with bound Thallium ions

Released:
Model geometry
Fit model/data
Source organism: Escherichia coli UTI89
Primary publication:
Use of thallium to identify monovalent cation binding sites in GroEL.
Acta Crystallogr Sect F Struct Biol Cryst Commun 65 967-71 (2009)
PMID: 19851000

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173032 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperonin GroEL Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 547 amino acids
Theoretical weight: 57.26 KDa
Source organism: Escherichia coli UTI89
Expression system: Escherichia coli
UniProt:
  • Canonical: Q1R3B6 (Residues: 2-548; Coverage: 100%)
Gene names: UTI89_C4741, groEL, groL
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 135.676Å b: 260.954Å c: 287.872Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.262 0.261 0.293
Expression system: Escherichia coli