3n2w

X-ray diffraction
1.45Å resolution

Crystal structure of the N-terminal beta-aminopeptidase BapA from Sphingosinicella xenopeptidilytica

Released:

Function and Biology Details

Reaction catalysed:
Cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-176035 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-peptidyl aminopeptidase BapA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 373 amino acids
Theoretical weight: 38.63 KDa
Source organism: Sphingosinicella xenopeptidilytica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q52VH2 (Residues: 30-402; Coverage: 100%)
Gene name: bapA
Sequence domains: Peptidase family S58
Structure domains: L-amino peptidase D-ALA esterase/amidase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 87.36Å b: 96.72Å c: 101.42Å
α: 90° β: 108.23° γ: 90°
R-values:
R R work R free
0.131 0.131 0.15
Expression system: Escherichia coli BL21(DE3)