› 1tzq

X-ray diffraction
2.3Å resolution

Crystal structure of the equinatoxin II 8-69 double cysteine mutant

Released:
DOI: 10.2210/pdb1tzq/pdb
PDB entry 1tzq coloured by chain, front view.
PDB entry 1tzq coloured by chain, side view.
PDB entry 1tzq coloured by chain, top view.
Source organism: Actinia equina
Primary publication:
Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich.
Kristan K, Podlesek Z, Hojnik V, Gutiérrez-Aguirre I, Guncar G, Turk D, González-Mañas JM, Lakey JH, Macek P, Anderluh G
J Biol Chem 279 46509-17 (2004)
PMID: 15322132

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158432 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DELTA-actitoxin-Aeq1a Chain: A
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 19.45 KDa
Source organism: Actinia equina
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61914 (Residues: 40-214; Coverage: 90%)
Sequence domains: Sea anemone cytotoxic protein
Structure domains: Cytolysin/lectin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 36.585Å b: 52.682Å c: 39.789Å
α: 90° β: 92.26° γ: 90°
R-values:
R R work R free
0.195 0.192 0.274
Expression system: Escherichia coli BL21(DE3)

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Citations

10 review citations

Biological functions of sphingomyelins.
Slotte JP. (2013)
9 more