› 4dwl

X-ray diffraction
2.69Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181203 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bbp7 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 131 amino acids
Theoretical weight: 15.01 KDa
Source organism: Bordetella virus BPP1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q775D7 (Residues: 1-128; Coverage: 100%)
Gene name: bbp7
Structure domains: 23S rRNA-intervening sequence

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
1 modified residue:
Ligand MSE 25 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 54.317Å b: 63.072Å c: 105.295Å
α: 90° β: 103.77° γ: 90°
R-values:
R R work R free
0.197 0.194 0.244
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Formylglycine, a post-translationally generated residue with unique catalytic capabilities and biotechnology applications.
Appel et al. (2015)
3 more

2 mentions without citation

Structure of the essential diversity-generating retroelement protein bAvd and its functionally important interaction with reverse transcriptase.
Alayyoubi et al. (2013)
1 more