› 2pn5

X-ray diffraction
2.7Å resolution

Crystal Structure of TEP1r

Released:
DOI: 10.2210/pdb2pn5/pdb
PDB 2pn5 coloured by chain and viewed from the front.
PDB 2pn5 coloured by chain and viewed from the side.
PDB 2pn5 coloured by chain and viewed from the top.
Source organism: Anopheles gambiae
Primary publication:
Structural basis for conserved complement factor-like function in the antimalarial protein TEP1.
Baxter RH, Chang CI, Chelliah Y, Blandin S, Levashina EA, Deisenhofer J
Proc. Natl. Acad. Sci. U.S.A. 104 11615-20 (2007)
PMID: 17606907

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 3 x NAG
Ligand NA 3 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P43212
Unit cell:
a: 150.515Å b: 150.515Å c: 226.315Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.239 0.275
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Mosquito Trilogy: Microbiota, Immunity and Pathogens, and Their Implications for the Control of Disease Transmission.
Gabrieli et al. (2021)
8 more

6 mentions without citation

Structural basis for conserved complement factor-like function in the antimalarial protein TEP1.
Baxter et al. (2007)
5 more