› 1fm2

X-ray diffraction
2Å resolution

THE 2 ANGSTROM CRYSTAL STRUCTURE OF CEPHALOSPORIN ACYLASE

Released:
DOI: 10.2210/pdb1fm2/pdb
PDB entry 1fm2 coloured by chain, front view.
PDB entry 1fm2 coloured by chain, side view.
PDB entry 1fm2 coloured by chain, top view.
Source organism: Brevundimonas diminuta
Primary publication:
The 2.0 A crystal structure of cephalosporin acylase.
Kim Y, Yoon K, Khang Y, Turley S, Hol WG
Structure 8 1059-68 (2000)
PMID: 11080627

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192214 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 18.57 KDa
Source organism: Brevundimonas diminuta
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9L5D6 (Residues: 30-198; Coverage: 25%)
Structure domains: Penicillin Amidohydrolase, domain 1
Glutaryl-7-aminocephalosporanic-acid acylase subunit beta Chain: B
Molecule details ›
Chain: B
Length: 520 amino acids
Theoretical weight: 58.69 KDa
Source organism: Brevundimonas diminuta
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9L5D6 (Residues: 199-718; Coverage: 75%)
Sequence domains: Penicillin amidase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 13 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P41212
Unit cell:
a: 73.6Å b: 73.6Å c: 380.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.208 0.23
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Quorum-quenching microbial infections: mechanisms and implications.
Dong et al. (2007)
5 more

4 mentions without citation

Cephalosporins as key lead generation beta-lactam antibiotics.
Lin et al. (2022)
3 more