› 1znt

Solution NMR

18 NMR structures of AcAMP2-Like Peptide with non Natural Fluoroaromatic Residue (AcAMP2F18Pff/Y20Pff) complex with N,N,N-triacetylchitotriose

Released:
DOI: 10.2210/pdb1znt/pdb
PDB entry 1znt coloured by chain, ensemble of 18 models, front view.
PDB entry 1znt coloured by chain, ensemble of 18 models, side view.
PDB entry 1znt coloured by chain, ensemble of 18 models, top view.
Source organism: Amaranthus caudatus
Primary publication:
On the importance of carbohydrate-aromatic interactions for the molecular recognition of oligosaccharides by proteins: NMR studies of the structure and binding affinity of AcAMP2-like peptides with non-natural naphthyl and fluoroaromatic residues.
Chávez MI, Andreu C, Vidal P, Aboitiz N, Freire F, Groves P, Asensio JL, Asensio G, Muraki M, Cañada FJ, Jiménez-Barbero J
Chemistry 11 7060-74 (2005)
PMID: 16220560

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Antimicrobial peptide 2 Chain: A
Molecule details ›
Chain: A
Length: 31 amino acids
Theoretical weight: 3.21 KDa
Source organism: Amaranthus caudatus
Expression system: Not provided
UniProt:
  • Canonical: P27275 (Residues: 26-55; Coverage: 49%)
Sequence domains: Chitin recognition protein

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
No bound ligands
1 modified residue:
Ligand PFF 2 x PFF

Experiments and Validation Details

Entry percentile scores
Refinement method: The structures are based on a total 314 cross peaks, 248 NOE-derived distance restraints, and finally 208 distance constraints and 18 come from cys-cys disulfide were used in the final round of calculation
Expression system: Not provided

Quick links

Citations

5 review citations

Binding mechanisms in supramolecular complexes.
Schneider HJ. (2009)
4 more

1 mention without citation

Stepwise Reversion of Multiply Mutated Recombinant Antitrypsin Reveals a Selective Inhibitor of Coagulation Factor XIa as Active as the M358R Variant.
Hamada et al. (2021)