› 1hi9

X-ray diffraction
2.4Å resolution

Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.

Released:
DOI: 10.2210/pdb1hi9/pdb
PDB entry 1hi9 coloured by chain, front view.
PDB entry 1hi9 coloured by chain, side view.
PDB entry 1hi9 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Structure of the Bacillus subtilis D-aminopeptidase DppA reveals a novel self-compartmentalizing protease.
Remaut H, Bompard-Gilles C, Goffin C, Frère JM, Van Beeumen J
Nat Struct Biol 8 674-8 (2001)
PMID: 11473256

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-aminopeptidase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 274 amino acids
Theoretical weight: 30.28 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P26902 (Residues: 1-274; Coverage: 100%)
Gene names: BSU12920, dciAA, dppA
Sequence domains: D-aminopeptidase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 10 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: C2221
Unit cell:
a: 145.11Å b: 165.86Å c: 109.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.268
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Folds and activities of peptidoglycan amidases.
Firczuk et al. (2007)
2 more

4 mentions without citation

Dependence of α-helical and β-sheet amino acid propensities on the overall protein fold type.
Fujiwara et al. (2012)
3 more