› 1mmc

Solution NMR

1H NMR STUDY OF THE SOLUTION STRUCTURE OF AC-AMP2

Released:
DOI: 10.2210/pdb1mmc/pdb
PDB entry 1mmc coloured by chain, ensemble of 26 models, front view.
PDB entry 1mmc coloured by chain, ensemble of 26 models, side view.
PDB entry 1mmc coloured by chain, ensemble of 26 models, top view.
Source organism: Amaranthus caudatus
Primary publication:
H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.
Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P
J Mol Biol 258 322-33 (1996)
PMID: 8627629

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antimicrobial peptide 2 Chain: A
Molecule details ›
Chain: A
Length: 30 amino acids
Theoretical weight: 3.19 KDa
Source organism: Amaranthus caudatus
UniProt:
  • Canonical: P27275 (Residues: 26-55; Coverage: 49%)
Sequence domains: Chitin recognition protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores

Quick links

Citations

7 review citations

The relationship between peptide structure and antibacterial activity.
Powers et al. (2003)
6 more

8 mentions without citation

Carbohydrate-binding modules: fine-tuning polysaccharide recognition.
Boraston et al. (2004)
7 more