› 1m24

X-ray diffraction
0.9Å resolution

Trichotoxin_A50E, An Ion Channel-Forming Polypeptide

Released:
DOI: 10.2210/pdb1m24/pdb
PDB entry 1m24 coloured by chain, front view.
PDB entry 1m24 coloured by chain, side view.
PDB entry 1m24 coloured by chain, top view.
Source organism: Trichoderma viride
Primary publication:
Model for a helical bundle channel based on the high-resolution crystal structure of trichotoxin_A50E.
Chugh JK, Brückner H, Wallace BA
Biochemistry 41 12934-41 (2002)
PMID: 12390019

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162306 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
TRICHOTOXIN_A50E Chains: A, B
Molecule details ›
Chains: A, B
Length: 19 amino acids
Theoretical weight: 1.67 KDa
Source organism: Trichoderma viride

Ligands and Environments

1 bound ligand:
Ligand CCN 2 x CCN
2 modified residues:
Ligand AIB 18 x AIB
Ligand VOL 2 x VOL

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS
Spacegroup: P1
Unit cell:
a: 9.49Å b: 16.85Å c: 31.68Å
α: 95.77° β: 98.07° γ: 99.45°
R-values:
R R work R free
0.076 not available 0.092

Quick links

Citations

7 review citations

Peptaibols and related peptaibiotics of Trichoderma. A review.
Szekeres et al. (2005)
6 more

2 mentions without citation

Molecular modeling of the reductase domain to elucidate the reaction mechanism of reduction of peptidyl thioester into its corresponding alcohol in non-ribosomal peptide synthetases.
Manavalan et al. (2010)
1 more