› 1l4v

Solution NMR

SOLUTION STRUCTURE OF SAPECIN

Released:
DOI: 10.2210/pdb1l4v/pdb
PDB entry 1l4v coloured by chain, ensemble of 18 models, front view.
PDB entry 1l4v coloured by chain, ensemble of 18 models, side view.
PDB entry 1l4v coloured by chain, ensemble of 18 models, top view.
Source organism: Sarcophaga peregrina
Primary publication:
1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin.
Hanzawa H, Shimada I, Kuzuhara T, Komano H, Kohda D, Inagaki F, Natori S, Arata Y
FEBS Lett 269 413-20 (1990)
PMID: 2401368

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148348 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sapecin Chain: A
Molecule details ›
Chain: A
Length: 40 amino acids
Theoretical weight: 4.09 KDa
Source organism: Sarcophaga peregrina
UniProt:
  • Canonical: P18313 (Residues: 55-94; Coverage: 56%)
Sequence domains: Arthropod defensin
Structure domains: Knottin, scorpion toxin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing

Quick links

Citations

17 review citations

Biological mediators of insect immunity.
Gillespie et al. (1997)
16 more

12 mentions without citation

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