3he1

X-ray diffraction
2.1Å resolution

Secreted protein Hcp3 from Pseudomonas aeruginosa.

Released:
Source organism: Pseudomonas aeruginosa
Primary publication:
Crystal structure of secretory protein Hcp3 from Pseudomonas aeruginosa.
J Struct Funct Genomics 12 21-6 (2011)
PMID: 21476004

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190823 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major exported protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 195 amino acids
Theoretical weight: 22 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HI36 (Residues: 1-172; Coverage: 100%)
Gene names: PA0263, PA1512, PA5267, hcpA, hcpB, hcpC
Sequence domains: Type VI secretion system effector, Hcp
Structure domains: Hcp1-like

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P312
Unit cell:
a: 141.219Å b: 141.219Å c: 105.052Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.214 0.254
Expression system: Escherichia coli BL21(DE3)