› 3sh8

X-ray diffraction
2Å resolution

Crystal structure of fluorophore-labeled beta-lactamase PenP in complex with cephaloridine

Released:
DOI: 10.2210/pdb3sh8/pdb
PDB entry 3sh8 coloured by chain, front view.
PDB entry 3sh8 coloured by chain, side view.
PDB entry 3sh8 coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Increased structural flexibility at the active site of a fluorophore-conjugated beta-lactamase distinctively impacts its binding toward diverse cephalosporin antibiotics.
Wong WT, Chan KC, So PK, Yap HK, Chung WH, Leung YC, Wong KY, Zhao Y
J Biol Chem 286 31771-80 (2011)
PMID: 21705325

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-133594 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 266 amino acids
Theoretical weight: 29.65 KDa
Source organism: Bacillus licheniformis
Expression system: Escherichia coli
UniProt:
  • Canonical: P00808 (Residues: 43-307; Coverage: 94%)
Gene names: blaP, penP
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
Ligand CED 2 x CED
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 43.33Å b: 91.73Å c: 66.11Å
α: 90° β: 104° γ: 90°
R-values:
R R work R free
0.228 0.225 0.267
Expression system: Escherichia coli

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Citations

1 review citation

Overcoming Aminoglycoside Enzymatic Resistance: Design of Novel Antibiotics and Inhibitors.
Zárate et al. (2018)
14 other articles

1 mention without citation

Influence of C-H...O interactions on the structural stability of β-lactamases.
Lavanya et al. (2013)