PDBe 1b65

X-ray diffraction
1.82Å resolution

Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-aminopeptidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 375 amino acids
Theoretical weight: 40.46 KDa
Source organism: Ochrobactrum anthropi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59632 (Residues: 1-375; Coverage: 100%)
Gene name: dmpA
Sequence domains: Peptidase family S58
Structure domains: L-amino peptidase D-ALA esterase/amidase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P21212
Unit cell:
a: 156.97Å b: 96.22Å c: 154.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.169 0.206
Expression system: Escherichia coli