› 1kec

X-ray diffraction
2.3Å resolution

PENICILLIN ACYLASE MUTANT WITH PHENYL PROPRIONIC ACID

Released:
DOI: 10.2210/pdb1kec/pdb
PDB entry 1kec coloured by chain, front view.
PDB entry 1kec coloured by chain, side view.
PDB entry 1kec coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural and kinetic studies on ligand binding in wild-type and active-site mutants of penicillin acylase.
Alkema WB, Hensgens CM, Snijder HJ, Keizer E, Dijkstra BW, Janssen DB
Protein Eng Des Sel 17 473-80 (2004)
PMID: 15254299

Function and Biology Details

Reaction catalysed: 
Penicillin + H(2)O = a carboxylate + 6-aminopenicillanate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139290 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Penicillin G acylase subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.85 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06875 (Residues: 26-234; Coverage: 25%)
Gene name: pac
Structure domains:
Penicillin G acylase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 557 amino acids
Theoretical weight: 62.44 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P06875 (Residues: 290-846; Coverage: 68%)
Gene name: pac
Sequence domains: Penicillin amidase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand GRO 1 x GRO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P1
Unit cell:
a: 50.781Å b: 64.226Å c: 64.543Å
α: 72.6° β: 73.86° γ: 73.56°
R-values:
R R work R free
0.154 0.151 0.206
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Kinetics of beta-lactam antibiotics synthesis by penicillin G acylase (PGA) from the viewpoint of the industrial enzymatic reactor optimization.
Giordano et al. (2006)
4 more

1 mention without citation

Engineering the substrate specificity of a thermophilic penicillin acylase from thermus thermophilus.
Torres et al. (2013)