3c7v

X-ray diffraction
2.07Å resolution

Structural Insight into the Kinetics and Delta-Cp of interactions between TEM-1 Beta-Lactamase and BLIP

Released:

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-lactamase TEM Chains: A, C
Molecule details ›
Chains: A, C
Length: 263 amino acids
Theoretical weight: 28.98 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P62593 (Residues: 24-286; Coverage: 100%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily
Beta-lactamase inhibitory protein Chains: B, D
Molecule details ›
Chains: B, D
Length: 165 amino acids
Theoretical weight: 17.46 KDa
Source organism: Streptomyces clavuligerus
Expression system: Escherichia coli
UniProt:
  • Canonical: P35804 (Residues: 37-201; Coverage: 100%)
Sequence domains: Beta-lactamase inhibitor (BLIP)
Structure domains: Beta-lactamase Inhibitory Protein; Chain:B, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CAMD BEAMLINE GCPCC
Spacegroup: P21
Unit cell:
a: 48.671Å b: 129.044Å c: 78.898Å
α: 90° β: 91.2° γ: 90°
R-values:
R R work R free
0.216 0.214 0.238
Expression system: Escherichia coli