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X-ray diffraction
3.2Å resolution

Translocator domain of autotransporter NalP from Neisseria meningitidis

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Autotransporter domain-containing protein Chain: X
Molecule details ›
Chain: X
Length: 308 amino acids
Theoretical weight: 32.08 KDa
Source organism: Neisseria meningitidis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GKS5 (Residues: 776-1083; Coverage: 29%)
Gene names: COH25_05710, nalP
Structure domains: Autotransporter beta-domain

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2221
Unit cell:
a: 57.43Å b: 84.893Å c: 122.983Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.215 0.298
Expression system: Escherichia coli