PDBe 1gk1

X-ray diffraction
2.4Å resolution

Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C

Released:

Function and Biology Details

Reaction catalysed:
(7R)-7-(4-carboxybutanamido)cephalosporanate + H(2)O = (7R)-7-aminocephalosporanate + glutarate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha Chains: A, C
Molecule details ›
Chains: A, C
Length: 153 amino acids
Theoretical weight: 16.94 KDa
Source organism: Pseudomonas sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P07662 (Residues: 36-188; Coverage: 22%)
Structure domains: Penicillin Amidohydrolase, domain 1
Glutaryl-7-aminocephalosporanic-acid acylase subunit beta Chains: B, D
Molecule details ›
Chains: B, D
Length: 522 amino acids
Theoretical weight: 58.34 KDa
Source organism: Pseudomonas sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P07662 (Residues: 199-720; Coverage: 76%)
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2
Unit cell:
a: 230.29Å b: 70.44Å c: 114.8Å
α: 90° β: 97.48° γ: 90°
R-values:
R R work R free
0.18 0.18 0.219
Expression system: Escherichia coli