3mbt

X-ray diffraction
2.6Å resolution

Structure of monomeric Blc from E. coli

Released:
Source organism: Escherichia coli K-12
Primary publication:
Structural and biochemical analyses reveal a monomeric state of the bacterial lipocalin Blc.
Acta Crystallogr D Biol Crystallogr 66 1308-15 (2010)
PMID: 21123871

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-141758 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer membrane lipoprotein Blc Chain: A
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 19.13 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A901 (Residues: 19-177; Coverage: 100%)
Gene names: JW4110, b4149, blc, yjeL
Sequence domains: Lipocalin-like domain
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: I4122
Unit cell:
a: 88.94Å b: 88.94Å c: 78.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.276
Expression system: Escherichia coli