PDBe 1uyn

X-ray diffraction
2.6Å resolution

Translocator domain of autotransporter NalP from Neisseria meningitidis


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
NalP Chain: X
Molecule details ›
Chain: X
Length: 308 amino acids
Theoretical weight: 31.85 KDa
Source organism: Neisseria meningitidis
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q8GKS5 (Residues: 776-1083; Coverage: 29%)
Gene name: nalP
Sequence domains: Autotransporter beta-domain
Structure domains: Autotransporter beta-domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P6122
Unit cell:
a: 57.97Å b: 57.97Å c: 346.435Å
α: 90° β: 90° γ: 120°
R R work R free
0.231 0.228 0.285
Expression system: Escherichia coli BL21(DE3)