› 1joh

X-ray diffraction
1.4Å resolution

THE STRUCTURE OF ANTIAMOEBIN I, A MEMBRANE-ACTIVE PEPTIDE

Released:
DOI: 10.2210/pdb1joh/pdb
PDB 1joh coloured by chain and viewed from the front.
PDB 1joh coloured by chain and viewed from the side.
PDB 1joh coloured by chain and viewed from the top.
Source organism: Emericellopsis
Primary publication:
The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide.
Snook CF, Woolley GA, Oliva G, Pattabhi V, Wood SF, Blundell TL, Wallace BA
Structure 6 783-92 (1998)
PMID: 9655831

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:
ANTIAMOEBIN I Chains: A, B
Molecule details ›
Chains: A, B
Length: 17 amino acids
Theoretical weight: 1.65 KDa
Source organism: Emericellopsis

Ligands and Environments

1 bound ligand:
Ligand MOH 23 x MOH
4 modified residues:
Ligand AIB 12 x AIB
Ligand DIV 4 x DIV
Ligand HYP 4 x HYP
Ligand PHL 2 x PHL

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 26.53Å b: 28.82Å c: 9.06Å
α: 88.9° β: 96.64° γ: 123.85°
R-values:
R R work R free
0.156 not available not available

Quick links

Citations

5 review citations

Aib residues in peptaibiotics and synthetic sequences: analysis of nonhelical conformations.
Aravinda et al. (2008)
4 more

2 mentions without citation

The role of hydrophobic interactions in positioning of peripheral proteins in membranes.
Lomize et al. (2007)
1 more