5da8

X-ray diffraction
3Å resolution

Crystal structure of chaperonin GroEL from

Released:
Model geometry
Fit model/data
Source organism: Chlorobaculum tepidum TLS
Entry authors: Chang C, Marshall N, Feldmann B, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

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-185126 (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, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b
Length: 545 amino acids
Theoretical weight: 58.16 KDa
Source organism: Chlorobaculum tepidum TLS
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8KF02 (Residues: 1-545; Coverage: 100%)
Gene names: CT0530, 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: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 138.996Å b: 159.781Å c: 228.823Å
α: 75.46° β: 90.51° γ: 91.22°
R-values:
R R work R free
0.232 0.23 0.263
Expression system: Escherichia coli