5gui

X-ray diffraction
1.2Å resolution

Crystal structure of the N-terminal Domain of Caseinolytic protease associated chaperone ClpC1 from Arabidopsis thaliana

Released:
Model geometry
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Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-190323 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein ClpC1, chloroplastic Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.98 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9FI56 (Residues: 94-238; Coverage: 16%)
Gene names: At5g50920, CLPC1, DCA1, HSP93-V, IRM1, K3K7.7
Sequence domains: Clp amino terminal domain, pathogenicity island component
Structure domains: Clp, N-terminal domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RRCAT INDUS-2 BEAMLINE PX-BL21
Spacegroup: P212121
Unit cell:
a: 40.1Å b: 44.29Å c: 97.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.147 0.167
Expression system: Escherichia coli BL21(DE3)