1lp1

X-ray diffraction
2.3Å resolution

Protein Z in complex with an in vitro selected affibody

Released:
Source organism: Staphylococcus aureus
Primary publication:
Structural basis for recognition by an in vitro evolved affibody.
Proc Natl Acad Sci U S A 100 3191-6 (2003)
PMID: 12604795

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
PDBe Complex ID:
PDB-CPX-153668 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Affibody binding protein Z Chain: A
Molecule details ›
Chain: A
Length: 58 amino acids
Theoretical weight: 6.45 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
Structure domains: Immunoglobulin FC, subunit C
Immunoglobulin G-binding protein A Chain: B
Molecule details ›
Chain: B
Length: 58 amino acids
Theoretical weight: 6.65 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P38507 (Residues: 212-269; Coverage: 12%)
Gene name: spa
Sequence domains: B domain
Structure domains: Immunoglobulin FC, subunit C

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P6122
Unit cell:
a: 55.546Å b: 55.546Å c: 155.749Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.225 0.224 0.256
Expression system: Escherichia coli