› 3ws0

X-ray diffraction
2Å resolution

N288Q-N321Q mutant BETA-LACTAMASE DERIVED FROM CHROMOHALOBACTER SP.560 (Condition-1A)

Released:
DOI: 10.2210/pdb3ws0/pdb
PDB entry 3ws0 coloured by chain, front view.
PDB entry 3ws0 coloured by chain, side view.
PDB entry 3ws0 coloured by chain, top view.
Source organism: Chromohalobacter sp. 560
Primary publication:
Structure of a highly acidic β-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs(+)-selective binding site.
Arai S, Yonezawa Y, Okazaki N, Matsumoto F, Shibazaki C, Shimizu R, Yamada M, Adachi M, Tamada T, Kawamoto M, Tokunaga H, Ishibashi M, Blaber M, Tokunaga M, Kuroki R
Acta Crystallogr D Biol Crystallogr 71 541-54 (2015)
PMID: 25760604

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 367 amino acids
Theoretical weight: 39.6 KDa
Source organism: Chromohalobacter sp. 560
Expression system: Escherichia coli
UniProt:
  • Canonical: Q76LX5 (Residues: 22-388; Coverage: 100%)
Gene name: bla
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
Ligand CA 10 x CA
Ligand CS 2 x CS
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P31
Unit cell:
a: 115.393Å b: 115.393Å c: 67.652Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.19 0.224
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Diversity and regulation of intrinsic β-lactamases from non-fermenting and other Gram-negative opportunistic pathogens.
Juan et al. (2017)
1 more

1 mention without citation

Structure of a highly acidic β-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs(+)-selective binding site.
Arai et al. (2015)