› 3qdh

X-ray diffraction
1.9Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fimbrial structural subunit Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 31.02 KDa
Source organism: Actinomyces naeslundii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O68212 (Residues: 199-488; Coverage: 58%)
Gene name: fimA
Sequence domains: Sgo0707 N2 domain
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU, APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 47.528Å b: 39.799Å c: 77.139Å
α: 90° β: 98.34° γ: 90°
R-values:
R R work R free
0.211 0.209 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

The scientific exploration of saliva in the post-proteomic era: from database back to basic function.
Ruhl S. (2012)
6 more

5 mentions without citation

Two autonomous structural modules in the fimbrial shaft adhesin FimA mediate Actinomyces interactions with streptococci and host cells during oral biofilm development.
Mishra et al. (2011)
4 more