› 1afp

Solution NMR

SOLUTION STRUCTURE OF THE ANTIFUNGAL PROTEIN FROM ASPERGILLUS GIGANTEUS. EVIDENCE FOR DISULPHIDE CONFIGURATIONAL ISOMERISM

Released:
DOI: 10.2210/pdb1afp/pdb
PDB entry 1afp coloured by chain, ensemble of 40 models, front view.
PDB entry 1afp coloured by chain, ensemble of 40 models, side view.
PDB entry 1afp coloured by chain, ensemble of 40 models, top view.
Source organism: Aspergillus giganteus
Primary publication:
NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism.
Campos-Olivas R, Bruix M, Santoro J, Lacadena J, Martinez del Pozo A, Gavilanes JG, Rico M
Biochemistry 34 3009-21 (1995)
PMID: 7893713

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-148152 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antifungal protein Chain: A
Molecule details ›
Chain: A
Length: 51 amino acids
Theoretical weight: 5.82 KDa
Source organism: Aspergillus giganteus
Expression system: Not provided
UniProt:
  • Canonical: P17737 (Residues: 44-94; Coverage: 70%)
Gene name: afp
Sequence domains: Antifungal protein
Structure domains: Antifungal protein domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

7 review citations

Regulation of gene expression by ambient pH in filamentous fungi and yeasts.
Peñalva et al. (2002)
6 more

5 mentions without citation

Antifungal Peptides of the AFP Family Revisited: Are These Cannibal Toxins?
Meyer et al. (2018)
4 more