2bsc

X-ray diffraction
1.4Å resolution

E. coli F17a-G lectin domain complex with N-acetylglucosamine, high- resolution structure

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 Chain: A
Molecule details ›
Chain: A
Length: 177 amino acids
Theoretical weight: 19.05 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
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
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P6122
Unit cell:
a: 42.483Å b: 42.483Å c: 272.952Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.202 0.251
Expression system: Escherichia coli BL21