› 1dy6

X-ray diffraction
2.13Å resolution

Structure of the imipenem-hydrolyzing beta-lactamase SME-1

Released:
DOI: 10.2210/pdb1dy6/pdb
PDB entry 1dy6 coloured by chain, front view.
PDB entry 1dy6 coloured by chain, side view.
PDB entry 1dy6 coloured by chain, top view.
Source organism: Serratia marcescens
Primary publication:
Structure of the imipenem-hydrolyzing class A beta-lactamase SME-1 from Serratia marcescens.
Sougakoff W, L'Hermite G, Pernot L, Naas T, Guillet V, Nordmann P, Jarlier V, Delettré J
Acta Crystallogr D Biol Crystallogr 58 267-74 (2002)
PMID: 11807251

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 29.39 KDa
Source organism: Serratia marcescens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54488 (Residues: 28-294; Coverage: 100%)
Gene names: SME12620_22, blaSME-1, blaSME-4, blaSME1, sme-2
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21
Unit cell:
a: 81.5Å b: 51.72Å c: 71.69Å
α: 90° β: 118.62° γ: 90°
R-values:
R R work R free
0.184 0.184 0.244
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Carbapenemases: the versatile beta-lactamases.
Queenan et al. (2007)
7 more

14 mentions without citation

Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.
Jeon et al. (2015)
13 more