› 5mn2

X-ray diffraction
2.35Å resolution

Cocrystal structure of Fc gamma receptor IIIa interacting with Affimer G3, a specific binding protein which blocks IgG binding to the receptor.

Released:
DOI: 10.2210/pdb5mn2/pdb
PDB 5mn2 coloured by chain and viewed from the front.
PDB 5mn2 coloured by chain and viewed from the side.
PDB 5mn2 coloured by chain and viewed from the top.
Source organisms:
Primary publication:
Affimer proteins inhibit immune complex binding to FcγRIIIa with high specificity through competitive and allosteric modes of action.
Robinson JI, Baxter EW, Owen RL, Thomsen M, Tomlinson DC, Waterhouse MP, Win SJ, Nettleship JE, Tiede C, Foster RJ, Owens RJ, Fishwick CWG, Harris SA, Goldman A, McPherson MJ, Morgan AW
Proc Natl Acad Sci U S A 115 E72-E81 (2018)
PMID: 29247053

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Low affinity immunoglobulin gamma Fc region receptor III-A Chains: A, B
Molecule details ›
Chains: A, B
Length: 175 amino acids
Theoretical weight: 20.08 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P08637 (Residues: 19-193; Coverage: 74%)
Gene names: CD16A, FCG3, FCGR3, FCGR3A, IGFR3
Sequence domains: Immunoglobulin domain
Structure domains: Immunoglobulins
Affimer G3 Chains: C, D
Molecule details ›
Chains: C, D
Length: 101 amino acids
Theoretical weight: 11.52 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

4 bound ligands:
Ligand NAG 7 x NAG
Ligand PEG 2 x PEG
Ligand GOL 1 x GOL
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P21
Unit cell:
a: 64.985Å b: 59.925Å c: 100.001Å
α: 90° β: 102.09° γ: 90°
R-values:
R R work R free
0.208 0.206 0.244
Expression systems:
  • Homo sapiens
  • Escherichia coli

Quick links

Citations

1 review citation

Toxin Neutralization Using Alternative Binding Proteins.
Jenkins et al. (2019)
10 other articles