› 2drw

X-ray diffraction
2.1Å resolution

The crystal structutre of D-amino acid amidase from Ochrobactrum anthropi SV3

Released:
DOI: 10.2210/pdb2drw/pdb
PDB entry 2drw coloured by chain, front view.
PDB entry 2drw coloured by chain, side view.
PDB entry 2drw coloured by chain, top view.
Source organism: Brucella anthropi
Primary publication:
Crystal structure and functional characterization of a D-stereospecific amino acid amidase from Ochrobactrum anthropi SV3, a new member of the penicillin-recognizing proteins.
Okazaki S, Suzuki A, Komeda H, Yamaguchi S, Asano Y, Yamane T
J Mol Biol 368 79-91 (2007)
PMID: 17331533

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase-related domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 363 amino acids
Theoretical weight: 40.13 KDa
Source organism: Brucella anthropi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9LCC8 (Residues: 1-363; Coverage: 100%)
Gene name: daaA
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand BA 23 x BA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P21
Unit cell:
a: 77.205Å b: 123.219Å c: 115.706Å
α: 90° β: 104.36° γ: 90°
R-values:
R R work R free
0.185 0.182 0.243
Expression system: Escherichia coli

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Citations

2 review citations

The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis.
Sauvage et al. (2008)
1 more