X-ray diffraction
2.5Å resolution

ATP-dependent Protease HslV from Bacillus anthracis str. Ames

Source organism: Bacillus anthracis str. Ames
Entry authors: Kim Y, Mulligan R, Kwon K, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
ATP-dependent cleavage of peptide bonds with broad specificity.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
ATP-dependent protease subunit HslV Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 183 amino acids
Theoretical weight: 19.74 KDa
Source organism: Bacillus anthracis str. Ames
Expression system: Escherichia coli
  • Canonical: Q81WK5 (Residues: 1-180; Coverage: 100%)
Gene names: BAS3681, BA_3968, GBAA_3968, hslV
Sequence domains: Proteasome subunit
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2
Unit cell:
a: 140.255Å b: 127.543Å c: 90.1Å
α: 90° β: 130.03° γ: 90°
R R work R free
0.166 0.165 0.204
Expression system: Escherichia coli