› 6pba

X-ray diffraction
1.77Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161951 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease ATP-binding subunit ClpC1 Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.53 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPC9 (Residues: 1-145; Coverage: 17%)
Gene names: MTCY07H7B.26, Rv3596c, clpC1
Sequence domains: Clp amino terminal domain, pathogenicity island component

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 44.53Å b: 59.12Å c: 58.79Å
α: 90° β: 97.49° γ: 90°
R-values:
R R work R free
0.197 0.195 0.223
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Acyldepsipeptide Analogues: A Future Generation Antibiotics for Tuberculosis Treatment.
Cobongela et al. (2022)
3 more

1 mention without citation

Structure of the N-terminal domain of ClpC1 in complex with the antituberculosis natural product ecumicin reveals unique binding interactions.
Wolf et al. (2020)