› 1apa

X-ray diffraction
2.3Å resolution

X-RAY STRUCTURE OF A POKEWEED ANTIVIRAL PROTEIN, CODED BY A NEW GENOMIC CLONE, AT 0.23 NM RESOLUTION. A MODEL STRUCTURE PROVIDES A SUITABLE ELECTROSTATIC FIELD FOR SUBSTRATE BINDING.

Released:
DOI: 10.2210/pdb1apa/pdb
PDB entry 1apa coloured by chain, front view.
PDB entry 1apa coloured by chain, side view.
PDB entry 1apa coloured by chain, top view.
Source organism: Phytolacca americana
Primary publication:
X-ray structure of a pokeweed antiviral protein, coded by a new genomic clone, at 0.23 nm resolution. A model structure provides a suitable electrostatic field for substrate binding.
Ago H, Kataoka J, Tsuge H, Habuka N, Inagaki E, Noma M, Miyano M
Eur J Biochem 225 369-74 (1994)
PMID: 7925458

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Antiviral protein alpha Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 29.77 KDa
Source organism: Phytolacca americana
Expression system: Not provided
UniProt:
  • Canonical: Q03464 (Residues: 22-285; Coverage: 97%)
Sequence domains: Ribosome inactivating protein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 47.1Å b: 116.3Å c: 49.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.172 not available
Expression system: Not provided

Quick links

Citations

2 review citations

Pokeweed antiviral protein, a ribosome inactivating protein: activity, inhibition and prospects.
Domashevskiy et al. (2015)
1 more

3 mentions without citation

Predicting the accuracy of protein-ligand docking on homology models.
Bordogna et al. (2011)
2 more