› 5cfa

X-ray diffraction
1.45Å resolution

Crystal structures of Bbp from Staphylococcus aureus with peptide ligand

Released:
DOI: 10.2210/pdb5cfa/pdb
PDB entry 5cfa coloured by chain, front view.
PDB entry 5cfa coloured by chain, side view.
PDB entry 5cfa coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structures of Bbp from Staphylococcus aureus reveal the ligand binding mechanism with Fibrinogen α.
Zhang X, Wu M, Zhuo W, Gu J, Zhang S, Ge J, Yang M
Protein Cell 6 757-66 (2015)
PMID: 26349459

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136016 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bone sialoprotein-binding protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 331 amino acids
Theoretical weight: 36.5 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14U76 (Residues: 272-598; Coverage: 30%)
Gene name: bbp
Sequence domains:
Structure domains:
Fibrinogen alpha chain Chains: C, D
Molecule details ›
Chains: C, D
Length: 15 amino acids
Theoretical weight: 1.67 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P02671 (Residues: 580-594; Coverage: 2%)
Gene name: FGA

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 60.916Å b: 74.961Å c: 75.563Å
α: 90° β: 102.91° γ: 90°
R-values:
R R work R free
0.18 0.178 0.212
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Staphylococcal Biofilm Development: Structure, Regulation, and Treatment Strategies.
Schilcher et al. (2020)
2 more

4 mentions without citation

Mechanical Stabilization of a Bacterial Adhesion Complex.
Huang et al. (2022)
3 more