› 4nk3

X-ray diffraction
1.9Å resolution

Amp-c beta-lactamase (pseudomonas aeruginosa) in complex with mk-7655

Released:
DOI: 10.2210/pdb4nk3/pdb
PDB entry 4nk3 coloured by chain, front view.
PDB entry 4nk3 coloured by chain, side view.
PDB entry 4nk3 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Discovery of MK-7655, a β-lactamase inhibitor for combination with Primaxin®.
Blizzard TA, Chen H, Kim S, Wu J, Bodner R, Gude C, Imbriglio J, Young K, Park YW, Ogawa A, Raghoobar S, Hairston N, Painter RE, Wisniewski D, Scapin G, Fitzgerald P, Sharma N, Lu J, Ha S, Hermes J, Hammond ML
Bioorg Med Chem Lett 24 780-5 (2014)
PMID: 24433862

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-150279 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 41.02 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: P24735 (Residues: 27-397; Coverage: 100%)
Gene names: PA4110, ampC
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand MK7 1 x MK7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 44.751Å b: 72.127Å c: 106.039Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.174 0.213
Expression system: Escherichia coli

Quick links

Citations

39 review citations

Colistin resistance in Klebsiella pneumoniae.
Ah et al. (2014)
38 more

4 mentions 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)
3 more