X-ray diffraction
1.65Å resolution

Crystal structure of a cleaved form of a chimeric receptor binding protein from Lactococcal phages subspecies TP901-1 and p2


Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
BPP; Receptor binding protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 136 amino acids
Theoretical weight: 14.84 KDa
Source organisms: Expression system: Escherichia coli
  • Canonical: Q9G096 (Residues: 33-63; Coverage: 19%)
  • Canonical: Q71AW2 (Residues: 163-264; Coverage: 39%)
Gene names: bpp, rbp
Structure domains: Phage tail base-plate Siphoviridae RBP, head domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 57.168Å b: 43.682Å c: 78.946Å
α: 90° β: 101.63° γ: 90°
R R work R free
0.165 0.164 0.201
Expression system: Escherichia coli