4wgl

X-ray diffraction
3.13Å resolution

Crystal structure of a GroEL D83A/R197A double mutant

Released:
Source organism: Escherichia coli K-12
Entry authors: Yang D, Fei X, LaRonde NA, Beckett D, Lund PA, Lorimer GH

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetradecamer (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: 548 amino acids
Theoretical weight: 57.26 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A6F5 (Residues: 1-548; Coverage: 100%)
Gene names: JW4103, b4143, groEL, groL, mopA
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 135.619Å b: 259.71Å c: 280.848Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.166 0.233
Expression system: Escherichia coli BL21