PDBe 1xxm

X-ray diffraction
1.9Å resolution

The modular architecture of protein-protein binding site

Released:
Primary publication:
The modular architecture of protein-protein binding interfaces.
Proc. Natl. Acad. Sci. U.S.A. 102 57-62 (2005)
PMID: 15618400

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-lactamase TEM Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 28.81 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: C, D
Molecule details ›
Chains: C, D
Length: 165 amino acids
Theoretical weight: 17.33 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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 45.706Å b: 124.473Å c: 156.951Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.247
Expression system: Escherichia coli