1zpl

X-ray diffraction
1.7Å resolution

E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me

Released:
Source organism: Escherichia coli
Primary publication:
Impact of natural variation in bacterial F17G adhesins on crystallization behaviour.
Acta Crystallogr. D Biol. Crystallogr. 61 1149-59 (2005)
PMID: 16041081

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
F17a-G fimbrial adhesin Chains: A, B
Molecule details ›
Chains: A, B
Length: 177 amino acids
Theoretical weight: 19.05 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99003 (Residues: 23-199; Coverage: 55%)
Gene name: f17aG
Sequence domains: Fimbrial adhesin F17-AG, lectin domain
Structure domains: Bacterial adhesins - F17c-type

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 42.805Å b: 42.805Å c: 288.244Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.208 0.254
Expression system: Escherichia coli