› 1zg6

X-ray diffraction
2.1Å resolution

TEM1 beta lactamase mutant S70G

Released:
DOI: 10.2210/pdb1zg6/pdb
PDB entry 1zg6 coloured by chain, front view.
PDB entry 1zg6 coloured by chain, side view.
PDB entry 1zg6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the wild-type TEM-1 beta-lactamase at 1.55 A and the mutant enzyme Ser70Ala at 2.1 A suggest the mode of noncovalent catalysis for the mutant enzyme.
Stec B, Holtz KM, Wojciechowski CL, Kantrowitz ER
Acta Crystallogr D Biol Crystallogr 61 1072-9 (2005)
PMID: 16041072

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase TEM Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 31.56 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P62593 (Residues: 1-286; Coverage: 100%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6
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: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 41.99Å b: 62.65Å c: 89.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.275
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

4 mentions without citation

Conserved water molecules stabilize the Omega-loop in class A beta-lactamases.
Bös et al. (2008)
3 more