› 5txv

X-ray diffraction
7.09Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent protease ATPase subunit HslU 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
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
Length: 442 amino acids
Theoretical weight: 49.53 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6H5 (Residues: 2-443; Coverage: 100%)
Gene names: JW3902, b3931, hslU, htpI
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 24 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 86.497Å b: 420.86Å c: 176.418Å
α: 90° β: 98.56° γ: 90°
R-values:
R R work R free
0.276 0.274 0.298
Expression system: Escherichia coli

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Citations

1 review citation

Mitochondrial AAA proteases: A stairway to degradation.
Steele et al. (2019)
1 other article