1e94

X-ray diffraction
2.8Å resolution

HslV-HslU from E.coli

Released:
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Mutational studies on HslU and its docking mode with HslV.
Proc Natl Acad Sci U S A 97 14103-8 (2000)
PMID: 11114186

Function and Biology Details

Structure analysis Details

Assemblies composition:
homo dodecamer
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-141352 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent protease subunit HslV Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 175 amino acids
Theoretical weight: 18.99 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A7B8 (Residues: 2-176; Coverage: 99%)
Gene names: JW3903, b3932, hslV, htpO, yiiC
Sequence domains: Proteasome subunit
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
ATP-dependent protease ATPase subunit HslU Chains: E, F
Molecule details ›
Chains: E, F
Length: 449 amino acids
Theoretical weight: 50.5 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6H5 (Residues: 2-443; Coverage: 100%)
Gene names: JW3902, b3931, hslU, htpI
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P6322
Unit cell:
a: 172.022Å b: 172.022Å c: 276.569Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.254 0.254 0.304
Expression system: Escherichia coli BL21(DE3)