› 4pm6

X-ray diffraction
1.56Å resolution

Crystal structure of CTX-M-14 S70G beta-lactamase at 1.56 Angstroms resolution

Released:
DOI: 10.2210/pdb4pm6/pdb
PDB entry 4pm6 coloured by chain, front view.
PDB entry 4pm6 coloured by chain, side view.
PDB entry 4pm6 coloured by chain, top view.
Source organism: Klebsiella pneumoniae subsp. pneumoniae HS11286
Primary publication:
Molecular basis for the catalytic specificity of the CTX-M extended-spectrum β-lactamases.
Adamski CJ, Cardenas AM, Brown NG, Horton LB, Sankaran B, Prasad BV, Gilbert HF, Palzkill T
Biochemistry 54 447-57 (2015)
PMID: 25489790

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101890 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 27.97 KDa
Source organism: Klebsiella pneumoniae subsp. pneumoniae HS11286
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H3H219 (Residues: 29-291; Coverage: 100%)
Gene name: KPHS_p301310
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 41.55Å b: 62.28Å c: 86.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.141 0.162
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamases.
Palzkill T. (2018)
2 more

2 mentions without citation

Molecular basis for the catalytic specificity of the CTX-M extended-spectrum β-lactamases.
Adamski et al. (2015)
1 more