› 1ajn

X-ray diffraction
2.36Å resolution

PENICILLIN ACYLASE COMPLEXED WITH P-NITROPHENYLACETIC ACID

Released:
DOI: 10.2210/pdb1ajn/pdb
PDB entry 1ajn coloured by chain, front view.
PDB entry 1ajn coloured by chain, side view.
PDB entry 1ajn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Ligand-induced conformational change in penicillin acylase.
Done SH, Brannigan JA, Moody PC, Hubbard RE
J Mol Biol 284 463-75 (1998)
PMID: 9813130

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: 23.84 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P06875 (Residues: 27-235; Coverage: 26%)
Gene name: pac
Structure domains:
Penicillin G acylase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 557 amino acids
Theoretical weight: 62.43 KDa
Source organism: 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 AAN 1 x AAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P1
Unit cell:
a: 52.12Å b: 65.08Å c: 76.3Å
α: 100.2° β: 111.44° γ: 105.81°
R-values:
R R work R free
0.152 0.152 0.218

Quick links

Citations

6 review citations

Modular enzymes.
Khosla et al. (2001)
5 more

3 mentions without citation

Cloning, overexpression, and characterization of a novel thermostable penicillin G acylase from Achromobacter xylosoxidans: probing the molecular basis for its high thermostability.
Cai et al. (2004)
2 more